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TEACHING BIOCHEMISTRY
IN THE
HIGH SCHOOL CLASSROOM

By

Van Albrecht Mchliiams

A THESIS

Submitted to
Michigan State University
in partial fulfillment of the requirements
for the degree of

MASTER OF SCIENCE

Department of Biological Science - Interdepartmental

1990

ABSTRACT

TEACHING BIOCHEMISTRY
IN THE
HIGH SCHOOL CLASSROOM

By

Van Albrecht McWiiliams

Recent dramatic developments in biochemistry and biotechnology
have resulted in more secondary schools becoming aware of the
necessity to address these two rapidly evolving areas. Citizens of
tomorrow will need to stay abreast of these developments - making
informed societal, political, and environmental decisions affecting
the future of our planet. The need for critical thinking and data
analysis skills by scientifically inclined students is crucial for
furthering their science education. The decisions to be made by
future scientist and potential world leaders are becoming increasingly
complex. This thesis is an attempt to bring biochemistry and
biotechnology to the high school classroom. Included are the
background, implementation. methods of instruction, evaluation data,
and conclusions of this study. The unit covers structure and function
of carbohydrates. lipids, proteins and enzymes, and nucleic acids.

Laboratory exercises, devoted to analysis, are emphasized.

TABLE OF CONTENTS

Introduction ......... ... .......................................... 1.
General Description of Unit 1.
Literature Survey 2.

Background 2.
Laboratory and Discussion 6.
Central Questions 8.
Goals of the Unit 8.
Key Unit Lists 10.
New or Important Terms and Concepts 10.
Real World Objects, Systems, and Techniques 10.
Unit Objectives 11.
Teaching Objectives 11.
Student Objectives 12.

Transformation. ... ....................... . ....................... 18.

Clinical Interviews 18.
Student Background Information - 18.
Analysis of Pre and Post Test Interviews 20.

Analysis of Unit Literature 22.
Do the Teaching Materials and Text Meet Objectives 22.

Does the Literature Reflect Full Scientific Understanding 24.
Does the Literature Raise or Address Common Misconceptions 24.

Instruction. . ................................................ 26.
Daily Calender and Detailed Outline of Lessons 26.
Innovative Methods 27.

Notes and Anecdotes 28.
Laboratory Exercise Outline 31.
Laboratory Techniques 32.
Laboratory Objectives 33.
Evaluation............. ......................................... 34.
Do Evaluation Instruments Reflect Each Objective 34.
Analysis of Test Data 34.
’Evidence that the Unit has Made a Difference 38.
Conclusion...... ...... . ................ ...... ................... .. 46.
Pertinent Events 46.
Accomplishments of the Unit 4?.
Suggested Revisions 49.
Suggested Future Units 49.
Glossary. ................. ..... ........... .............. .......... 51.
Appendices. ....... ........... ... ........... . ........... ... ..... 56.
Appendix A - Outline for Chemistry 11 56.

Appendix B — Daily Journal 65.

Iii

Appendix C Biochemistry Pre and Post Interview 74.
Appendix D Pre Test and Post Test 77.
Appendix E Unit Oulzzes 85.
Appendix F Unit Test 91.
Appendix G Special Assignments 120.
Appendix H Sample Overheads and Visuals 123.
Appendix 1 Sample Labs 133.
Bibliography.... ................................................ . 145.
General References ............................................... 147.

TABLE OF CONTENTS - CONT.

iv

Table 1
Table 2
Table 3

Table 4

LIST OF TABLES

Pre and Post Interview Results
Pre Test Results
Post Test Results

Regular Classroom Test Results

21.
39.
40.

42.

LIST OF FIGURES

Figure 1 - Average Pre Test and Post Test Results

vi

41.

INTRODUCTION

Wham

This thesis is based upon two years of research in teaching an
eleven week biochemistry unit to second year chemistry students. Two
years ago - In the summer previous to the 1988-89 school year - the
author developed a second year chemistry course for Stockbridge,
Michigan schools. This course was designed to offer college bound
students a much stronger and more diverse chemistry background. The
biochemistry unit in the original outline for the course included:
carbohydrates, lipids, proteins and enzymes, nucleic acids, and
buffers. Evaluation of the original outline suggested that buffers be
moved into the titration and pH unit. (see outline for Chemistry II -
Appendix A) This allowed students to have a good working knowledge of
buffers before beginning the biochemistry unit. Therefore, buffers
will be discussed minimally.

The main approach of the biochemistry unit is to provide an
introduction to the principles of biochemistry - giving students a
command of the concepts, the language, and an appreciation for the
process of discovery in biochemistry. The unit emphasizes a
laboratory approach, with 40 percent of class time in the laboratory
setting. Many modern research techniques are utilized. Pre- and
post interviews were conducted for the entire unit to determine
student background, the strengths and weaknesses of the unit, and

student comprehension. Pre- and post tests, designed to address the

stated objectives were also used for individual sections of the unit.

A Complete item analysis is included in the evaluation section.

W

Background

The idea for this research project evolved from the initial
Molecular Biology Workshop for Honors High School Teachers offered by
Michigan State University (sponsored by the National Science~
Foundation) during the summer of 1987 and subsequent research based
upon workshop outcomes during the summer of 1988. The workshop
emphasized: 1) biochemistry - in which Biochemistny by Stryer (1981),
was used as the textbook, and 2) laboratory technique - incorporating
current technologies. Subsequent research in the summer of 1988 also
involved a twofold emphasis. First, to execute, revise, edit, and
publish laboratory exercises developed by the-previous summer’s
participants, which resulted in IHE_!QRLD_QE_EIQ§HEMISIRX. a computer
software disk containing ten lab exercises for the high school
classroom. Second, to develop a specific unit using these labs and
other techniques for our individual classrooms.

After the author developed the outline, objectives, and
laboratory exercises, his next consideration was to find a text
feasible for the secondary level. The author presently uses flgdgnn
Chemistcy by Metcaif, Williams, and Castka (1986). While the text
does not have a unit on biochemistry, the Teacher’s Resource Book does

include a complete unit with six separate worksheets covering all the

areas required. The material is fairly comprehensive and easily

supplemented. Supplemental texts obtained for this unit Include:

Biochemistry 2nd ed. by Lubert Stryer, 1981.

3
Schaum’s Outline Series Biochemistry by Xuchel and Ralston, 1988.

Harper’s Biochemistry by Murray, Granner, Hayes, and Rodweil,
1986.

Biochem1§t[x_gf_Lipid§_ang_uembnanes by Vance and Vance, 1985.
Ing_Qngm1st;y_gf_§a£pgn_§gmpggflg§ by David E. Newton, 1986.
B1Qteghnglggy_1n_£g£§2e§tlye by David B. Sattelle, 1990.
nggenn_fllglggy by Otto and Towle, 1985.
ExeLg1sg§_1n_Biglggiga1_§gjgngg§ by Merle K. Heidemann, 1985.

Biochemistry_ZQQ (lecture illustrations) published by the
Department of Biochemistry, Michigan State University.

While the supplemental material was not entirely limited to these
publications, there is certainly more than enough quality information
to be gleaned for any secondary biochemistry course.

Having compiled these sources, I surveyed current literature
hoping to find pertinent information on teaching biochemistry at the
secondary level. In virtually everything I read there were two
recurring themes. One, that biochemistry is advancing in today’s
technology: and two, critical thinking and data interpretation is
essential for our scientifically inclined students.

The ‘explosion’ of biochemistry has resulted in more secondary
schools becoming aware of the need to address this area. Maler (1986)
stated that, “Biochemistry is a fascinating subject formally reserved

for graduate students only. ...this subject is now incorporated into

the secondary school curriculum in many places'' (p. 239). Maler
discussed practical illustrations of the topical approach to teaching
biochemistry. She includes three separate experiments that use
differing reagents to find the one that properly fits to solve ‘the
puzzle’. Parson (1986) writes: “In the past decade, the power and
scope of recombinant DNA technology have become apparent. Media
coverage of potential medical applications and financial success
stories have captivated students’ lmaginations.‘I Parson describes the
development of a topics course that stresses laboratory techniques and
methods with implications in the political, social, ethical, and
economic realms. Caruthers (1985) discusses the state of DNA
technology in the mid 1970’s, and states:

Even 10 years ago the chemical synthesis of DNA was a

time-consuming, cumbersome task ...(yieldlng) short DNA

segments containing 10 deoxynucleotldes or less. Now simple

methods are available for the rapid synthesis of relatively

large DNA fragnents (100-200 monomers each)... (p. 577).
Present techniques have sequenced more than 26 million bases of DNA
(Smith 1989). Illustrating the need for biochemical education at the
secondary level Grunwald (1986) wrote:

... the life sciences, especially biology and biochemistry,

should be considered in connection with the development of

chemical curricula, because the actual problems with which

humanity is confronted are becoming increasingly complex.

To teach chemistry, one must teach fundamentals... in

technical chemistry, biochemistry, and biotechnology.

(p. 775)
This article is a synopsis of the discussion held on chemical

curricula - one of the four main topics at the 1985 International

Conference on Chemical Education. Included in this article is an

application and an experiment showing how biotechnology can be
integrated into a regular chemistry course.

Shapiro and James (1980) in a survey about biochemical lecture
and laboratory requirements of 120 colleges and universities within
the Middle Atlantic Region, found: less than one third of the
institutions offered a biochemistry major, library holdings of
biochemistry journals were (at best) sparse, and only a limited number
of biochemistry laboratory texts had been published. The same survey
given today would probably yield equally interesting results.

Dramatic changes have taken place in this rapidly expanding field, as
summarized in the statement by Vance and Vance (1985): “Biochemistry
has matured to the point that advanced textbooks In the various
subcategories are required.“

Critical thinking and data analysis were key aspects of this unit
and were prompted by several observations. 'Scientific literacy Is
basic for living, working, and decision making in the 19805 and
beyond“ (NSF, 1982, p. 4). The obligation of today’s science
educators will be to develop scientific and technological literacy for
all students. 'in the teaching of basic biochemistry, ...it is
important to draw concise, easy-to-understand diagrams and schemes,
...in order to stress fundamental aspects within a unified framework'
(Macarulla and Marlno, 1985, p.79). Somewhat surprisingly, the author
found many students have yet to reach a well developed reasoning
stage. Mensch (1989) arrived at a similar observation and also noted:

In a world where genetic engineering and molecular biology
are becoming ever more Important, the development of a

thorough understanding of protein synthesis is vital.
Teaching this highly abstract concept to students, many whom

6

have not yet reached formal reasoning... is made more
difficult by the lack of good ‘hands-on’ instructional
aids. (p. 2)

After recognizing the need for easily understood diagrams and schemes
as well as manipulative models to aid in critical thinking, this

author had to construct methods to help students achieve these levels.

Streitberger (1988) asserts:

Recognizing the importance of this type of reflective and
critical thinking, (science based societal issues) a number
of state and national groups have encouraged the following
goals for the high school curriculum. These goals, ...
include: (1) 'to prepare students to use science and
technology in understanding and Improving (students’) daily
lives“, (2) 'to apply scientific knowledge to everyday life:
'and to introduce social and environmemtal implications of
scientific and technological development“, (3) IIto use
current societal issues and problems to meet the needs of
our society and of students“, (4) “to emphasize at all
levels the social and human relevance of chemistry“, and (5)
'to use attitudes and knowledge about science to live as an

informed citizen in a scientifically developed nation'.
(p. 60)

Laboratory and Discussion

Literature was also surveyed to find discussion units and
laboratory exercises. Many discussion units and extra readings were

taken from the previous list of supplemental texts. For example:

Stryer’s= Biochemistry
- enzyme substrate catalysis, pgs. 107-110.
- cholesterol as a precursor, pgs. 469-71, 473-79.
- membrane lipid bilayer, pgs. 210-13.
Vance and Vance: Wrens:
- cholesterol and coronary disease, pgs. 209-10.
- membrane lipid bilayer, pgs. 25-28.
Otto and Towle: flggg;n_fllglggy
- all of chapter seven on nucleic acids and protein
synthesis, pgs. 99-114.

Other discussion units Include: “Long Arm of the Lab,“ an article on
DNA fingerprinting from the Detzglt_£ngg_finess, Science and Medicine
section, (Jan. 10, 1989) and “Construction of a Restiction Map of the
Bacteriophage Lamda,“ an article on electrophoresis by Suelter (1989).
Discussion of articles was followed by an electrophoresis
demonstration. An oral report on steroid abuse by athletes was
required of students, giving them the opportunity to do their own
literature search.

Laboratory units were taken in most part from Ibe_flgn1d_gf
W and from Wm. Other labs
include "Qualitative Analysis Of Proteins and Alpha Amino Acids“ from
the Kemtec Educational Corporation, distributed by Carolina Biological
Supply, and “Properties of DNA“ from Modern Biology, Inc. Subsequent
labs, including this one, have been ordered for next year from Modern
Biology, Inc. (For a complete listing of all laboratory exercises see
the laboratory exercise outline on page 31.)

Preparing for laboratory exercises that were above the typical
chemistry setting, this author searched for some guidelines. The

following guidelines appeared in an article by Falk (1989):

Ideally, laboratory courses in the (undergraduate) freshman
chemistry curriculum should fulfill several purposes.

1. The laboratory experience should reinforce chemical
principles discussed in the course with “real“ examples.

2. The laboratory experience should teach the student how to
observe and describe a physical phenomenon and the logical
approach to solving a scientific problem.

3. If given a certain amount of freedom to experiment, a
student should be able to explore a chemical phenomenon to a
greater depth by trying related experiments on his or her
own.

There is an extensive list of adaptable high quality laboratory
exercises in today’s literature. The key questions in choosing these
are: What will serve the objectives best? Will the exercises fit the
time frame of the lab? Can the exercises be accomplished with the
available materials?

Hands on laboratory experiences are highly valued by our high
school Science Department. Our high school science committee has set
a minimum standard of 20 percent of class time in the laboratory. Our
science teachers adopted this standard in the spring of 1988 based on
the following recommendation by the National Science Foundation (NSF).
'Time on laboratory and field work ...Senior high school level: a
minimum of one instructional period per week, 20 percent of science
instruction time in the laboratory or field“ (NSF, 1982, p. 4). The
second year chemistry course, as stated previously, doubles this
requirement. The reason for this was to better address the two
re-occurring themes: the biotechnological explosion and the need for

critical thinking and data interpretation.

Winn:

Goals of the Unit

The author’s main classroom goal is to produce science literate
citizens. However, in Chemistry 11 my primary goal is to motivate
students to choose a science-related area as a career. Many excellent
students are turned off by “boring“ high school science experiences.
The hope is to rectify these previous “boring“ experiences and then

re-kindle an interest for those students who have been alienated by

science. In improving teaching skills, this author can use the new
and innovative Ideas that have been recently obtained to stimulate
student curiosity and eliminate apathy in lecture, discussion, and
laboratory settings. Ideally, this new background in teaching
techniques and subject matter will lead to better student
comprehension and make learning science fun and exciting. The author
also has the conviction that high school students need to see what
college classes are like. For this particular unit the author tried
to teach in a manner similar to a college course, with nearly as many
hours In laboratory as in lecture. Hopefully, students will be
‘turned on’ by the promising results of biotechnology as presented in

this course and summarized in the following.

Sattelle (1990) states:

Biotechnology’s potential is enormous: its promise
unrivaled. As a field of scientific research and commercial
enterprise, biotechnology has grown dramatically in the past
several years. Not surprisingly, the general public’s
understanding of what “biotechnology“ means has failed to
keep pace with this progress. This has resulted in a lack
of full appreciation of the implications of biotechnological
research and development... Improved healthcare, a more
abundant food supply, safer chemicals and a cleaner
environment can all be realized through the science of
biotechnology. (p. iv)

The major emphases for this unit - the central themes to be addressed
- are for students to acquire: a working knowledge of biochemical
concepts, a command of the technical or scientific language, exposure

to a wide variety of biotechnological techniques, and an appreciation

for the processes of discovery in biochemistry. These themes hold

10

promise of achieving student feedback toward the main goal of

motivating students to choose science-related careers.

WW3;

KEY UNIT LISTS

Upon completion of this unit students will be able to define and

demonstrate an understanding of the following terms and concepts.

Alcohols

Alpha amino acids
Antibody
Anticodons
Biochemistry
Biosynthesis
Carbohydrates
Carbonyl group
Catalyst
Cellulose

Chitin
Cholesterol
Codons

Coenzyme
Cofactor
Conjugated enzyme
Conjugated proteins
Dehydration synthesis
Denaturation
Digestion
Disaccharide

DNA

Enzyme

Essential amino acids
Ester

Fats

Fatty acids
Glycerol
Glycogen

Hormone

Hydrogen bonding
Hydrolysis
Hydrophllic
Hydrophobic
Hydroxyl group
Lipids
Metabolism
Monosaccharlde
mRNA

Neutral lipids
Nucleic acids
Nucleosldes
Nucleotides

Oil
Oligosaccharide
Organic molecules

WWW

Pectin

Peptides
Phospholiplds
Polypeptides
Polysaccharlde
Prosthetic group
Protein
Regulator
Replication

RNA

rRNA

Simple enzyme
Simple proteins
Starch

Steroids
Substrate
Transcription
Translation
tRNA

Waxes

The student will be able to explain how the following have

contributed to our understanding of biochemistry or how biochemistry

has contributed to our understanding of the following:

11

Assays Enzymatic Catalysis
Biotechnology Gel Permeation Chromatography
Centrifugation Genetic Duplication
Diet Heart Disease
Dietary Fiber Health
Dietary Role of: Metabolic Pathways
Carbohydrates Nutrition
Lipids Protein Synthesis
Proteins Role of Vitamins
Digestive Processes Spectrophotometry
DNA Fingerprinting Steroid Abuse
DNA Sequencing Thin Layer Chromatography
Electronmicroscopy X-Ray Crystallography

Electrophoresis
Energy Transformations

UNIT OBJECTIVES

W

1. To develop a new teaching module in biochemistry covering
four major areas: carbohydrates, lipids, proteins and enzymes,
and nucleic acids. These topics, covering a nine to twelve week
period, are to be included as part of a new second year chemistry

course with a major emphasis on laboratory work.

2. To accumulate background information on students - review
prior information and disseminate new, incorporating the
knowledge students have from their previous biology and chemistry

classes.

3. To determine student accomplishment through pre-testing and

post-testing.

12

4. To make chemistry a real world subject - emphasizing

biochemistry, thus providing a unique approach to chemistry

education.

5. To increase student awareness in the diversity of chemistry
and its related fields by using and/or demonstrating selected new

technology available to today’s researchers.

6. To provide students the opportunity to work with varied
materials and multiple approaches in specific areas of
biochemistry - thus planting the idea that these students are
capable of ‘modern’ research and becoming a scientist of

tomorrow.

7. To determine the overall effectiveness of the new modules -
by revising and reviewing the modules to determining what worked

well and what didn’t - using a student survey and test analysis.

W

W

Upon completion of this section, the student will be able to:

\

1. Define and demonstrate an understanding of the following

terms: biochemistry, biosynthesis, and organic molecules.

13

2. State: the essential elements of life; the importance of
water and carbon dioxide to life: how minerals are absorbed; the

four main classes of compounds of living matter.

3. Distinguish between organic and inorganic compounds.

W

Upon completion of this section, the student will be able to:

1. Define and demonstrate an understanding of: carbohydrates,
hydroxyl group, carbonyl group, hydrolysis, dehydration
synthesis, monosaccharide, disaccharide, Oligosaccharide,

polysaccharide, starch, glycogen, cellulose, pectin, and chitin.

2. List: the five common monosaccharides; the three important

disaccharides: the five important polysaccharides.

3. State: the composition of carbohydrates: the three main
classes of carbohydrates and their structural differences: the
five important polysaccharides and their functions; the other
name for glucose; the function of monosaccharides,

oligosaccharides, and polysaccharides.

4. Differentiate: classes of carbohydrates: types of

monosaccharides: types of disaccharides.

5. Identify: an hydroxyaldehyde and/or an hydroxyketone.

6. Explain: hydrolysis and dehydration synthesis.

14

7. Compare: the calorie content per gram with lipids and

proteins.

Liam:

Upon completion of this section, the student will be able to:

1. Define and show an understanding of: lipids, fatty acids,
alcohols, neutral lipids, phosphollpids, hydrophobic,
hydrophilic, waxes, steroids, fat, oil, glycerol, ester, and

cholesterol.

2. List: the four classes of lipids; the five common steroids.

3. State: the composition of lipids: the four major functions of
lipids; the specific functions of neutral lipids, phosphollpids,

waxes, and steroids.

4. Identify: the structure of glycerol: the general structure of
neutral lipids, phosphollpids, waxes, and steroids: the specific

structure of cholesterol, testosterone, and vitamin D.

5. Explain: saturated and unsaturated fatty acids: the

difference between fats and oils: hydrogenation.

6. Draw: the cell membrane and include all key components.

7. Compare: the calorie content per gram with carbohydrates and

proteins.

15

W

Upon completion of this section, the student will be able to:

1. Define and demonstrate an understanding of: protein, enzyme,
alpha amino acids, catalyst, regulator, hormone, antibody,
essential amino acids, peptides, polypeptide, simple proteins,
conjugated proteins, prosthetic group, denaturation, simple
enzyme, conjugated enzyme, cofactor, coenzyme, digestion,

metabolism, and substrate.

2. List: the functions of proteins: the factors affecting enzyme
catalyzed reactions: the characteristics of protein molecules;

the causes of denaturation.

3. Give an example of: each of the functions of proteins; a

cofactor and a coenzyme.

4. State: the composition of proteins: the basic building blocks
of proteins: the most abundant organic molecules within living
cells: the two main classes of proteins: the two main classes of
enzymes: what the symbol [ 1 represents: the importance of the
essential amino acids: how the essential amino acids that we

don’t have are obtained.

5. Explain: how peptides and polypeptides are formed: protein

metabolism: protein digestion: amino acid biosynthesis.

6. Describe: how proteins control cell structure and function:

how the enzyme substrate complex works in biochemical reactions:

16

where each of the following enzymes work and which'substrate they

act upon: amylase, lipase, pepsin, trypsin, and peptidase.

7. Identify: the twenty common amino acids from their

abbreviations.

8. Draw: the general formula for alpha amino acids and label all
key components: an enzyme substrate complex showing how the
enzyme causes the sustrate to break apart and how an enzyme can

combine two substrate molecules.

9. Compare: the calorie content per gram with carbohydrates and

lipids.

W

Upon completion of this section, the student will be able to:

1. Define and show an understanding of: nucleic acids,
nucleotides, DNA, RNA, mRNA, rRNA, tRNA, nucleosides,
replication, hydrogen bonding, codons, anticodons, transcription,

and translation.

2. List: the three types of RNA.

3. State: the two main functions of nucleic acids: the
contributions of Franklin, Watson and Crick: the chemical nature
of nucleic acids: what each of the types of RNA represent: mRNA,
tRNA and rRNA.

4. Identify: the structure of AMP, ADP and ATP.

*Ii*

17

5. Complete: the proper sequence for a given strand of DNA and a

strand of RNA.

6. Describe: the composition of nucleic acids; where specific
pyrimidines and purines are found: the base pairings for DNA and

RNA: the formation of DNA and RNA.

7. Explain: the role of ADP and ATP: the function of DNA and

RNA: the five step process of protein synthesis.
8. Compare: the structure and function of DNA to RNA.
9. Draw: a section of DNA - include at least six bonds with

proper base pairing: the basic tRNA structure and label.

Students are expected to demonstrate an understanding of all

terms on both tests and laboratory exercises.

TRANSFORMATION

Clinical intecylgws
Student Background Information

The first step in conducting the student interviews was to gather
background information. This information included: age, sex, grade,
G.P.A., and educational background. Educational background was
divided into schools attended and previous secondary science classes.
Because all of my students wished to participate and the classes were
small - 11 students in ’89 and 12 students in ’90 - all students were
interviewed. The average age of the ’89 class was 17.3 years with
ages ranging from 16 to 18. The average age in ’90 was 17.4 with the
range being 17 to 19. The ratio of females to males was 3:8 in ’89
and 6:5 in ’90. There was one Junior and ten seniors in the ’89
class, while there were three Juniors and nine seniors in the ’90
class. The average G.P.A. in ’89 was 3.47 ranging from 2.75 to 4.0
and 3.49 in ’90 with a range of 3.0 to 4.0. All students, except
one, had attended Stockbridge High School throughout their high school
years. All students attended middle school in the district, with the
same exception: one third had attended elementary school in other
districts. Biology and Chemistry I were taken by the total (23
students) of both classes. Most students (14) had taken - or were
taking - Physics. Approximately half had taken Earth Science.
One-fifth had taken Physical Science and only two students had Anatomy
and Physiology. Other nominal science classes were Human Science
(Health) and General Biology.

18

19

Next, this author was curious about the students’ educational and
personal goals. The questions encompassed plans for furthering their
education, area(s) of interest - major/minor, and career goals. Every
student planned on continuing his/her education. Two were planning to
attend Junior college while the remainder planned on attending a four
year institution. The colleges most frequently named were: Michigan
State University (7), Michigan Tech (4), and the University of
Michigan and Central Michigan University (3) each. Only one student
was going out of state: to the University of Depaul. Upon completion
of this unit, fifteen of the twenty three students chose a science as
their main area of interest. They listed these majors and minors as
their choices:

Chemistry - 4

Physics - 2

Environmental Engineering - 2

Biochemistry

Bio-Physics

Medicine

Sports Medicine

Dietary Nutrition

Areospace Engineering

Electical Engineering

Computer Engineering

Environmental Conservation
Other majors and/or minors were: Business Law (3), Math, Accounting,
and Journalism. Three students had yet to decide but were leaning
toward science. Many students hadn’t reached a decision on career
goals. Comments were, for the most part, that they wanted to
complete a year or two of college before making such an important

decision. However, there were a few students who felt they had firmly

decided. One felt she would pursue a medical career, placing her

20

emphasis on developing new medicines. One student was certain that he
was going to pursue biochemistry as a career. Another student was
sure she wanted to be an Environmental Engineer. Bio-Physics was the

career choice of a fourth student.
Analysis of Pre and Post Test Interviews

After gathering the background and educational goals, the author
used a pre-test, post test format to determine how much prior
biochemistry knowledgestudents had and then compared with the post
test interview to see if the unit had indeed made a difference. The
interview form is included in appendix C. For this section, the
author wrote down student responses as close to verbatim as possible
and then waited to evaluate them when all pre-interviews were
completed. The same format was followed for the post interview. To
protect the integrity of the interview, the author simply asked the
questions and made no comments whatsoever until each response was
completed. The responses were evaluated as if the students were being
graded for a regular test, with the exception of no partial credit.

The interview consisted of a set of 20 questions. Average
pre-test scores for ’89 and ’90 were 3.18 and 2.72 respectively.
Average post test scores were 14.22 and 13.44 for ’89 and ’90. The
results are given in Table 1. Recall there are 11 students in the ’89

class and 12 students in ’90.

21

Table 1 Pre and Post Interview Results

Scores are listed in the format of ’89/’90 for correct responses.

For example: a score of 2/5 under the heading ’89/’90 would
represent two students in 1989 gave correct responses and five
students in 1990 answered the question correctly.

 

(not including last three questions)

i Pre-test Post test
I Questions (condensed) ’89/’90 ’89/’90
I

I What is Biochemistry? 3/3 6/7

I What is Biosynthesis? 1/1 5/6

I Four classes of organic coumpounds. 0/0 8/7

I Major use of carbohydrates? 7/8 9/11
I Carbohydrates contain? 9/5 11/9

I Three main classes of carbohydrates. 0/0 8/6

I How does glycogen differ from starch? 0/0 4/3

I Largest use of lipids by humans? 4/6 8/7

i Tryglycerldes are commonly called? 4/2 9/6

l Main function of waxes? 3/3 9/11
l Two examples of common steroids. 0/0 11/10
I Element found in proteins but not ... 3/3 11/11
I Basic building block of proteins. 1/2 10/9

I Define conjugated protein. 0/0 5/3

I Enzymes are catalyst for digestion and ... 0/1 5/3

I What is meant by denatured protein? 0/0 10/12
l DNA and RNA are responsible for ... 0/0 6/10
I Define replication, transcription ... 0/0 7/9

I What are buffers? 5/6 9/10
I Three key areas of physiological...buffers. 2/4 6/8

I Why is Biochemistry important to you? 6/4 8/11
I Why is Biochemistry important to mankind? 7/6 9/10
I How has this unit aided you for college? - 8/10
l Average total scores 3.2/2.7 14.2/13.4
I

I

 

The results of this survey show that the students’ major prior
infocmation concerned the function of carbohydrates and carbohydrate
composition. Average scores on the post interview show that
substantial learning had indeed taken place. The questions for the
most part were consistent with the stated objectives: however, there

were some exceptions. One exception was: “How does glycogen differ

22

from starch?“ which is an ambiguous question. Students were unclear
whether they were being asked for structure or function. “Define
conjugated enzyme.“ had many responses that were close, but if
students did not specifically use the term ‘prosthetic group’ they
were not given credit. “Enzymes are catalysts for digestion and...“
also had some ambiguity, with many ‘respiration’ responses instead of
the correct response: ‘metabolism’. The question “Largest use of
lipids by humans?“ would have been answered correctly by all students
had the author accepted ‘cell membranes’ in addition to the expected
answer: ‘energy storage’. The questions covering buffers indicated
the necessity for a brief review. Over 88 percent of the students had
developed an appreciation for Biochemistry and considered it important
to them personally and to mankind. Nearly 80 percent of the students
felt this unit would be beneficial to their college careers.

One major omission of the interview was the total absence of
questions concerning laboratory investigations. With 40 percent of
class time being allocated to this crucial area, the author would
certainly suggest laboratory questions be included. This omission was

definitely a major mistake.
Wt:
Do the Teaching Materials and Text Meet Objectives?

The “Teacher’s Resource Book“ that accompanied the course text

had worksheets that covered most of the objectives. However, each

23

section did require a certain amount of supplemental material. The
two sections that required the most additional material were lipids
and nucleic acids. Supplemental materials for all sections are
discussed in the following paragraphs.

Other areas the worksheets covered did not include the importance
of: hydrogen bonding, buffers in living systems, the electron
transport system, photosynthesis, bloenergetics, and the role of ATP,
ADP, and AMP. (see Appendix H)

The lion’s share of the supplemental material was presented as
overheads and used primarily for discussion. The author’s purpose was
to introduce the complexity of biochemistry, make important
connections resulting in better student comprehension, and present the
complexity of biochemistry without demanding students assimilate extra
information. Stressing career opportunities throughout the discussion
of supplementary materials was a key point. Additional discussion
elements for carbohydrates contained the digestion, absorption, and
metabolism of carbohydrates, including the functional role of
glycogen. The lipid supplementary material covered-fatty acids,
digestion and absorption of lipids, lipid transport in blood, role of
cholesterol, energy from lipids, biosynthesis of lipids, and hormones.
Structure of the cell membrane’s lipid bilayer was covered at length
as it was not included in the worksheets. Proteins and enzymes
required two handouts. Protein structure was definitely deficient and
needed help. A handout from Newton (1986) covered this well. Protein
digestion and metabolism were also discussed as well as amino acid

biosynthesis. A handout elaborating on the enzyme-substate complex

24

was included from Stryer (1981). A number of overheads were necessary
to complement the nucleic acid section. Cellular characteristics, the
flow of genetic information, nucleotides, key elements of DNA
structure, the functional classes of RNA, transcription and
translation, and mutations were improved upon or introduced. Students
were given a Mggenn_Biglggy text and required to read the chapter on

nucleic acids and do the end of chapter assignment.

Does the Literature Reflect Full Scientific Understanding?

Analyzing the teaching literature for content is vital for the
success of the unit. The key of the author’s analysis was to see if
the whole of the objectives were covered. Any omissions in the text
and re-enforclng materials must be covered. This author feels the
biochemistry worksheets satisfactorily meet the objectives stated in
the introductory section. Supplementary materials, for the most part,
were necessary to bring about a more complete understanding of
biochemical processes. If students were expected to meet objectives
covering the areas of metabolism and digestion for example, this would
add at least three to four weeks to the unit and place demands upon
them that are unrealistic. The lone exception was the omission of the
lipid bl-layer of cellular membranes. This concept is well within the
grasp of secondary students and the author believes it is vital to a

basic understanding of biochemical processes.

Does the Literature Raise or Address Common Misconceptions?

25

Misconceptions are the major roadblock to student learning.
Nowhere is this more apparent than in the teaching of science.
Complete texts have addressed this issue. Driver, Guesne, and
Tiberghien (1985) found students’ conceptions have several general
features. These features are: perceptually dominated thinking,
limited focus, linear causal reasoning, undifferentiated concepts,
context dependency, and predominant conceptions. To expect any
educator to address all of these features is, of course, ludicrous.
Nonetheless, any quality educator must keep these thoughts in mind
when helping students tackle difficult and/or abstract concepts.

The worksheet text contained two considerable misconceptions.
First, it was stated cholesterol was a steroid. This notion was
misleading for students. Cholesterol is the metabolic precursor for
the five major classes of steroids (Stryer, 1981). This misconception
was fully addressed and hopefully corrected. The second misconception
presented in the text stated that waxes were also steroids. Waxes are
a class of neutral lipids composed of long chain alcohols and fatty
acids. This issue was also addressed in discussion. When discussing
and correcting misconceptions with students I emphasized that authors
have varying opinions and texts are frequently edited, leaving out
valuable information.

One benefit of teaching this unit for students was their response
regarding that being a scientist or laboratory technichlan is not as
boring as previously perceived. The emphasis on biotechnology and the
subsequent discussions certainly aided in clearing up this common

misconception.

INSTRUCTION

WWW

Chemistry II Journal - Biochemistry

The journal encompasses the daily calendar of the unit and a
detailed outline of the lessons and methods of presentation. The
lecture outline for the entire course is in appendix A. Appendix A
includes buffers which were covered earlier in the course and reviewed
at the beginning of this unit. Samples of laboratory exercises,
overheads, special assignments, and visuals are listed in the daily
journal (Appendix B) and placed in separate appendices. (Appendices G,
H, and I) The pre and post interview, pre-test and post test, regular
quizzes and regular test are also included in the appendix.

(Appendices C - F) Below is a sample of the daily journal.

Day - 1 Monday: 2-12-90

LESSON PLAN

Introduction to Biochemistry

Pre-Test: Carbohydrates (appendix D)

Assignment: Read worksheet #1 - ‘The Chemistry of Living
Things’

Review: Buffers and their physiological importance

- (appendix A) .

Lecture notes and discussion: see outline (appendix A)
Teaching assists - overhead projector, blackboard, &
visuals (appendix H)

Homework: Ouestions 1-9 worksheet 1

Day - 2 Tuesday: 2-13-90

LESSON PLAN
Correct homework and discuss
Finish lecture
Homework: Handout “Long Arm Of The Lab“ - DNA

Fingerprinting Article from The_ngtnglt_£;eg_£;gs§
Students are to read, summarize and include their

26

2?

opinion of this ‘state of the art technique’ as
permitted by the courts to use as evidence.

Day - 3 Wednesday: 2-14-90
LESSON PLAN
Collect DNA Fingerprinting summary
Discussion: article itself, grading procedure - content,
grammar, spelling, punctuation, and clarity.
Demonstration: How gel electrophoresis works
Handout: “Construction of a Restriction Map of the
Bacteriophage Lambda“ - article on electrophoresis by
Dr. Clarence Suelter, M.S.U.
Homework: Worksheet #2 ‘Carbohydrates’ read for tomorrow.
xxx Samples of visuals, overheads, special assignments, and
laboratory exercises are included in the appendix. Each is listed in

the daily journal for easier access. (Appendix B)

Innovative Methods

Having a small class lends itself to easier applications of
innovative methods. Demonstrations can be viewed ‘up close’ by all
students. One of the more innovative areas the author tries to
maintain is the introduction of new or up-to-date laboratory
techniques. In order to save money, a laboratory exercise can be
performed as a demonstration rather than by the entire class.
Although a demonstration is not the prefered method, for small classes
it can be accomplished successfully. Three demonstrations that the
author does for students, executed as demonstrations rather than
‘hands on’ laboratory exercises are: electrophoretic techniques,
partition chromatography, and gel permeation chromatography. The
author believes the requirement that students spend 40 percent of

their class time In laboratory is also quite innovative. This allows

28

students the opportunity to pursue in depth many of the lecture
tapics. Students get added experience in laboratory practices
benefitting them as college freshmen.

Small classes are also more manageable for small group work.
Many homework and review assignments are handled in small groups when
the students are ‘creating’ the assignment material. This small group
work is implemented before all major test and for difficult homework
assignments: this encompasses 15-20% of class time. chussion amongst
peers is beneficial for increased learning because questioning
students receive feedback from fellow students which for many is
easier to assimilate. Learning is also aided in small groups by
students having to search for answers rather than getting a quick ‘in
one ear and out the other’ response from their teacher. Students get
better acquainted with each other and are more likely to risk making
an incorrect statement. Discussion is also easier to elicit from
students. Discussion is a major priority with this author. When
students carry out discussions however, misconceptions may occur, but
they can be easily corrected. Good discussion also gives the
instructor an excellent indication of what the students understand

about the topic(s).
Notes and Anecdotes

DNA Fingerprinting was a true success with students. Using the
two articles “Long Arm of the Lab“ and “Construction of a Restriction
Map of the Bacteriophage Lambda“ in conjunction with the

electrophoresis demonstration peaked in a high level of interest, a

29

lively discussion, and even a minor debate. The debate centered on
the theme that even the best trained laboratory technichlans can make
mistakes and that lawyers can somehow always come up with their own
‘experts’ to refute findings. Clearly students retained a good deal
of knowledge on electrophoresis and DNA sequencing.

When students were asked for someone to explain or define the
term ‘assay’ - even though these students have some familiarity with
this term - the normal response is no show of hands, or at best a
roundabout guess. Therefore, I developed a way of helping them to
remember. First, I simply tell them the common definition: “The
qualitative or quantitative analysis of a substance.“ Next, I ask if
everyone is comfortable with this definition: normally most students
nod or respond affirmatively. Then I write the word ‘ASSESS’ on the
board in big capital letters. 1 then say: “to assess something is to
analyze, correct? (lots of nods) Now an ‘assay’ is nothing more than
a way to assess (point to the word on the board) a substance. For
when you do an assay, do it very carefully so you do not end up
looking like ----(pause)“ and I quickly erase the last ‘8’ in ASSESS.
Now, I certainly have everyone’s attention. However, the remaining
word on the board is not one to be left in plain view. So, I quickly
erase the word and someone invariably says: “I don’t get it,“ which
puts the rest of the class in stitches. By the time a fellow student
explains to this person, order is pretty well restored. Epilogue:
The term ‘assay’ is now well - if not permanently - etched in their

minds.

30

The protein digestion lab led to a real eye opener for one young
man. When I asked him, “Has there been much of any sign that
digestion has taken place?“ the student replied, “No, not much. The
gelatin Is still seven millimeters across.“ I then replied, “Determine
the surface area of the piece of gelatin now as compared to the full
ten millimeter square you started with.“ He did, and his response was
non-verbal. He just looked wide-eyed and wore a very sheepish grin,
to which I replied, “Do you still say there has not been much of a
change?“ The young man responded, “No, I’d say there’s been quite a
change.“ I simply smiled in approval and moved on to the next station
to ask the same question.

While reviewing proteins, in particular conjugated proteins, my
students had a good laugh at my expense. I used the term ‘prostrate’
group instead of prosthetic group and the classroom burst into
laughter, including me. Laughter can certainly be said ‘to be the
best medicine’. The ensuing discussion was lively and - to say the
least - full of smiles.

A major benefit these students receive is the familiarity they
obtained with modern laboratory techniques and equipment. These
Included - but were not limited to - Oualitative Assays, Ouchterlony
Diffusion, Spectrophotometric Techniques, Electrophoretlc Techniques,
Chromatographic Techniques, Hydrogen Ion Equilibrla, Acid and
Enzymatic Hydrolysis of Starch, and Determining the Physical
Properties of DNA. Ouchterlony Diffusion and Hydrogen Ion Equilibria‘
were not included in the biochemistry unit. Nonetheless, students did

perform these labs earlier in the year. Student comments and

31

reactions were very favorable. They commented that they enjoyed the
variety and the ‘newness’ of these techniques. Students conveyed they
are more comfortable with attempting complex scientific tOplcs and

current laboratory techniques.

We

Nine exercises make up the laboratory section of this unit. Two
of the laboratory exercises were completed as demonstrations due to a
lack of materials. Most of the exercises took multiple class periods
to complete. Only the ‘Fat Digestion’ lab could be completed in one
laboratory period. The ‘Study of Saccharides’ lab took five days to
complete. In total, 19 days were committed to laboratory work.
Dividing this number by the actual number of classroom sessions - 48,
a total of 40 percent of class time was spent in the laboratory
setting. The following is a list of the laboratory exercises and
their location in the appendix.
Pre-Lab: Study of Saccharides
Saccharides
General Effect of Salivary Amylase on Starch
Introduction to Spectrophotometry
Digestion of Fat
Introduction to Qualitative Analysis of

Proteins and Amino Acids

Partition Chromatography of Amino Acids
. Protein Digestion by Papain and Bromelain

Gel Permeation Chromatography
. Properties of DNA

000% O‘OIACDNH

H

Labs #3, #4, #8 and #9 were taken from Ine_flgn1d_gf Biochemistry
software disk. Lab #2 and lab 87 were obtained from Exgngisg§_ln

Biglgglgal_§gjgnge. The pre lab #1 was developed by Sonja Mlchaud (my

32

student teacher in ’89) and revised by the author. Lab #5 was
developed by the author. Lab #6 was obtained through Carolina
Biological Supply and lab #10 was acquired from Modern Biology, Inc.

I now have over 100 laboratory exercises covering biochemistry
and biotechnology. Which I will gladly share with anyone who requests
them. Lipids is the one area where laboratory exercises are scarce.

A list may be obtained by contacting the author. Address: Stockbridge

High School, 416 North Clinton, Stockbridge, Michigan 49285.

Laboratory Techniques

Laboratory techniques emphasized in the saccharide lab are:
Iodine Test, Benedict’s Test, Acid Hydrolysis, and Enzymatic
Hydrolysis. For the salivary amylase lab spectrophotometry or
calorimetry is the technique used. The ‘Introduction to
Spectrophotometry’ lab stresses spectrophotometry and graphing. The
fat and protein digestion labs also emphasize Enzymatic Hydrolysis.
The qualitative analysis lab incorporates the use of Assays to
identify specific proteins and amino acids. Paper chromatography and
determination of R. values are the key techniques used in ‘Partition
Chromatography’. The ‘Gel Permeation Chromatography’ lab is a unique
separatory technique for the secondary level. Determination of the
physical properties of DNA offers students techniques of spooling,

denaturation, and enzymatic hydrolysis.

33

Laboratory Objectives.

Upon completion of this section the student will be able to:

1. Determine: whether certain saccharides are reducing sugars:
if sugars are helically coiled or branched polysaccharides: the
effect of enzyme hydrolysis and acid hydrolysis upon
polysaccharides: the end products of fat digestion: the effect of
pH on enzymatic action: the R; value of an amino acid in a given

solvent: the effects of DNAase on the structure of DNA.

2. Discover: the physical changes that occur during starch

digestion: the physical properties of DNA.

3. Practice: the use of the spectrophotometer and eventually
master its use upon completion of lab exercises: spoollng

techniques as a means of separation.

4. Graph: the visible absorption spectrum of a colored solution.

5. Plot: a graph and interpolate results: and develop a standard

curve.

6. Explain: how lipase and bile work together in the breakdown

of fats: the enzymatic breakdown of a protein.

7. Assay: for identification of proteins and amino acids: for
determining an unknown protein or amino acid: for determining

denaturation of a single strand of DNA.

8. Separate: amino acids using paper chromatography.

EVALUATION

W

The pre and post test instruments do not reflect each objective:
they are shortened versions of the regular classroom test which does
cover the full spectrum of objectives. Students’ grades were not
affected by pre and post test scores. Grades were only based upon
regular classroom work. However, post test could be used as part of
the overall grade. The pre and post test instruments were designed to
include a broad sampling of objectives. The reasoning behind this was
that pre and post test covering all objectives would take nearly a
full period to complete and students would bemoan such an exercise.
Full cooperation of the students to put forth their best efforts was
essential for the results to be meaningful. Therefore the instruments
were intentionally kept short to attain a higher level of quality
student effort. Pre and post test instruments were used in previous
units to acquaint students with the concept of testing for analysis.
Early results indicated that some students simply wrote in an answer
just to finish the test as fast as possible. Fortunately, most of the
students cooperated well. While the uncooperative ones dropped the
course at semester break - before the biochemistry unit. The pre and

post tests are included in Appendix D.

AW

An item analysis was conducted for each of the pre and post
tests. The answers were keyed on scantron sheets and an item analysis
processed in the Computer Laboratory at Michigan State University was

34

35

completed. Item analysis is useful in guiding and improving
instruction. According to Olson (1990), a minimum number of 50 test
will yelld the best analysis. This study was by necessity, conducted
on class sizes of 11 and 12 respectively. However, the item analysis
statistics were beneficial to the author and did indicate several key
results which are discussed later.

Item analysis breaks the students’ scores into groups. The
groups are divided into the upper, middle , and lower groups. This is
done to determine an “index of discrimination“. The index of
discrimination is the difference between the proportion of the upper
group with correct responses and the proportion of the lower group
with correct responses. Olson (ibid) states: “It has long been
accepted that optimal item discrimination is obtained when the upper
and lower groups each contain twenty-seven percent of the total
group.“ (p. 1). The higher the discrimination index, the more
discriminating the question. The difficulty Index is the proportion
of the total group who answered the question item incorrectly. A high
difficulty index indicates that the question is difficult while a low
index indicates an easy question. Olson also noted: “...most test
constructors desire items with indices of difficulty no lower than 20
nor higher than 80, with an average ...from 30 or 40 to a maximum of
60.“ (p. 2). Using these two indices, the author was able to look for
ambiguity, level of difficulty, and poor option alternatives in the
individual test questions.

The item analysis of the post test helped to determine student

performance in meeting the objectives. Findings included: all tests

36

would have been more meaningful had they consisted of twenty questions
(see Appendix D): and that it is very difficult to include four
suitable alternative distractors (options) for certain questions. In
addition, questions with low indices of difficulty (20 or less)
presented a dilemma: were the questions too easy or does this indicate
that objectives were met by a high percentage of students. None of
the tests had items that reflected an ambiguous question. This is
evident by the fact that none the lower group scores were higher than
the upper group for any question. The results are very subjective due
to the small size of the groups. The pre-test results give much
better ranges within the indices than the post test. However, one
finds it very difficult to analyze instructional methods based upon
scores achieved before material was eveh presented. Completing the
item analysis, the author arrived at the following results for each
section of the unit.

The carbohydrate test consisted of 15 questions containing three
items from the laboratory objectives. Five of the questions for the
’89 group had low difficulty indices. In analyzing these questions,
the author felt number 4 would be considered an easy question and the
others simply indicate students had met the objectives. The ’90 group
had two questions with low difficulty indices, questions 4 and 10.
This suggests that #4 is indeed an easy question. Questions 3, 4, and
12 had indices of discrimination of zero for both years. However,
question #3 has a fairly high index of difficulty in ’90 which means

that the middle group students missed the question instead of the

lower group. Question 812 is definitely a problem, with indices of

37

difficulty of 100 and 91 respectively and discriminations of zero.
This question needs correcting. While the correct response was there
(‘5), the students had chosen response #2 - which was only partially
correct. Rather than being an ambiguous question, which is normally
indicated by such results, the responses were ambiguous and the item
can easily be corrected by revising response #2. This should give a
much better range in the item analysis. The remaining questions,
based on the analysis, fit the desired indices fairly well.

For the remaining sections on lipids, proteins and enzymes, and
nucleic acids, the analysis will be based on both years combined to
give a somewhat better indication of test item quality. For the
results on the tests see Table 2.

The lipid test contained ten questions with one item from the
laboratory objectives. Questions 2, 6, and 9 had indices of
difficulty and discrimination of zero for both years. Did these
results indicate easy questions or were objectives met by all
students? The author feels they are all viable questions. Pre-test
scores give no indication of ‘easy question’ items and anyone taking
the test without a background in ‘llpids’ would be fortunate to guess
one of three. Question #5 fits the ‘ideal’ test item very well.
Students chose three of the four other optional responses and both
indices were fairly high and within the recommended range. There was
no indication of a very difficult question or one that was ambiguous.

The protein and enzyme test consisted of 20 questions with only
one item concerning a laboratory objective. Only question 14 had low

indices for both difficulty and discrimination. This question upon

38

examination is easy for students based upon the very poor quality of
the other options (distractors). These distractors certainly need to
be changed, or at the very least, Improved upon. When developing test
its imperative to carefully choose all distractors. Question #4 was a
difficult question. The index of difficulty in ’89 was 100 and 58 in
’90. Analysis of the question showed that the question was designed
to be difficult and required ‘critical thinking’ on the part of
students. The ’90 group showed improvement on this question and the
index of discrimination was 100, indicating only the ‘thinkers’ got
the question correct. Item #4 was also a well balanced test item
having students choose all four other options. The remaining items
fit the desired indices fairly well.

The nucleic acid test was the last of the pre and post test. The
test contained 15 items, none of which included a laboratory
objective. Questions 4, 5, and 15 have low indices of difficulty and
discrimination. The pre-test indices are all high for these three
questions and upon evaluation of the items, none were considered easy.
The students had met these three objectives very well. Question
number 6 in the ’89 group showed good option balance but in ’90 all of

the students but one had correct responses.

Wampum

The following tables and figure are illustrations of the results
students attained after completing this unit. Pre-test and post test
results for both years are included in Tables 2 and 3. Table 4 shows

the results for both years of the students’ regular classroom tests.

39

Figure 1 represents the pre-test and post test comparisons for both
years. Tables 2-4 and Figure 1 reflect combined class averages. Pre

test and post test are included in Appendix D.

Table 2 - Pre Test Results

Results reflect 23 combined scores for ’89 and ’90.

 

Test Topics Carbohydrates Lipids Proteins Nucleic acids

I l
l I
l & Enzymes I
I l
I Pre-Test ’89 A ’90 I
i Total questions 15 10 20 15 I
I Mean score 9.08 4.59 8.09 4.51 I
I Percentage 61 46 40 30 I
I St. Deviation 2.34 1.47 2.88 1.39 I
I Range 4-13 1-7 2-14 2-7 I
l I
I

441

 

The carbohydrate test scores on the pre-test in ’89 were inflated
due to students not taking the test until five days into the unit.
This was the fault of the instructor as it was nearly forgotten. The
pre-test scores in ’90 were also somewhat inflated as the reading
assignment had been completed prior to the test. Thus the average
scores do not reflect a ‘true’ pre test score. Fortunately, these

errors did not occur in the other units.

40

Table 3 - Post Test Results

Results reflect 23 combined scores for ’89 and ’90.

 

Test Topics Carbohydrates Lipids Proteins Nucleic acids

I I
I I
I & Enzymes l
l I
I Post Test ’89 A ’90 I
I Total questions 15 10 20 15 I
I Mean score 9.73 8.39 14.03 11.71 I
l Percentage 65 84 70 78 I
I St. Deviation 2.58 1.33 3.73 2.82 I
I Range 6-14 5-10 8-20 3-15 I
I I
J l

 

The average score on the carbohydrate post test is not reflective
of student achievement. The results of the carbohydrate post test
(class average of 57%) were disappointing for the class of ’90. This,
the author feels, is a direct result of student apathy toward post
test and this ‘lack of effort’ was subsequently addressed. The post
test results in ’89 showed an average of 73 percent which is within
the ‘normal’ percentage for the secondary classroom. Combining the
two averages, a percentage of 65 was obtained. Four students did
achieve a score of 14 correct indicating positive results.

The lipid test scores were better than expected on the post tests
and Indicate that a great deal of learning had occurred. With class
percentages going from 49 to 85 in ’89 and from 43 to 83 in ’90 the
author was very pleased with the results. However, the author’s
enthusiasm was somewhat tempered by the brevity of the test. A test
half again as long, or better yet, even twice as long would be a much
more accurate indicator of student achievement. Five of the total 23

students did receive perfect scores of 10.

 

 

.mmoazo'wcnmxi aommxoo

16.6 '

AVERAGE F‘FCE TEST fil-ID F‘U'ST TEST RESULTS

 

12.8 " "fl ‘

 

 

 

 

 

 

 

 

F‘FIE TEST
FEI'ST TEST

 

 

 

T"

”HUI: m:

    

NAME OF TEST

 

'Figure 1 - Average Pre Test and Post Tests Results

41

 

42

The protein and enzyme post test also indicated marked
improvements over the pre-test. Combined average percentages for the
two pre-tests were 40 percent and for the post test the combined
averages were 70 percent. One score of 19 was recorded for ’89 and
one score of 20 was achieved in ’90. The protein and enzyme test is
the better indicator of student learning as the average scores are
based upon 20 questions rather than 10 or 15 as in the other tests.

The results on the nucleic acids test are also encouraging. The
test scores improved from 28 to 73 percent in ’89 and from 32 to 83
percent in ’90. The mean score improvement on the post test of 1.59
in ’90 is significant. The author feels this resulted from additional
supplementary materials and an improved laboratory exercise. There

were four perfect scores of 15, two in each year.

Table 4 - Regular Classroom Test Results

Results reflect 23 combined scores for ’89 and ’90.

 

Test Name Carbohydrates Lipids Proteins Nucleic Acids
8 Enzymes

Regular Test ’89 8 ’90

Total points 62 68 75 65
Mean score 46.81 54.45 55.10 51.35
Percentage 76 80 74 79
St. Deviation 6.79 9.59 11.58 9.98
Range 30-56 33-67 39-72 22-65

h——-————_———

 

Table 4, summarizes the results of the regular classroom test.
The author believes that regular classroom tests are accurate

indicators of student performance, since these test scores greatly

43

affect students’ grades. The regular test encompasses nearly all
objectives, both lecture and laboratory. The mean for the regular
test scores is 68. Multiple choice, short answer, matching, listing,
explaining, defining, analyzing, and interpreting questions were used.
Laboratory objectives were extensively included. The complete set of
tests is included with answer keys in Appendix F.

The main purpose in including the regular test results is to add
validity to the post test. By comparing the percentages on the
regular tests with the post tests, one is able to see that the post
test results are indeed valid. The four test result percentages of
the post test and regular test match up favorably. The one exception
in the results is the carbohydrate test comparison. There is a
difference of 13 percent in post test and regular test percentages.
The author noted this discrepancy to the class - asked them to give a
complete effort on the pre and post test - and based upon the
remaining test comparisons, this effort seems to have occurred.

Evidence of student interest came in ‘unmeasurable’ forms.
Students would come into class before and after school to re-do or
improve laboratory exercises. Students, interested in specific areas,
would request additional readings and there were even a few requests
for additional labs. The highlight of the year occurred when two
seniors, who had the last week off, came back into the class for three
out of the five days to do additional laboratory work: staying for two
hours or’more performing titrations and other analysis techniques.

A discussion during the lipid unit led to the discovery of a

common misconception among high scool students. The statement was

44

made by one of the students that fats in any form are ‘bad’ for you.
Many students agreed. An animated discussion ensued involving all
students: after emphasizing all of the functions of lipids and the
necessity of lipids for body processes, the misconception was
corrected.

The final evidence came during the post interviews. Nineteen of
the twenty three students gave very good to excellent answers to the
questions - “Why is biochemistry Important to you?“ and “Why is
biochemistry important to mankind?“. The final question on the post
interview was - “How do you think this unit will benefit you in your
college science courses? Eighteen of the twenty three students felt
this unit and the preceding units would be of great benefit for
college. Some of their comments included: “I’m planning on going into
medicine and I no longer have nearly the level of fear for the
difficulty of the classwork and labs.“ “I was planning on majoring in
Genetics but now I’ve switched to Bio-physics.“ “I was thinking about
majoring in Chemistry, now I’m planning on it!“ This was a good
indication that students were indeed motivated to choose science as a
career. The few who felt that this unit really wouldn’t help in
college were going into a business related curriculum. However,
several of these students did comment that the study requirements were
good preparation for the rigors of college classes.

Fortunately, there was not a large quantity of negative evidence.
Each year there were two students who I could not seem to motivate and
get them truly interested in biochemistry. Whether they did not care

for the material or ‘seniorltis’ had set in, the author remains

45

disappointed in their performance. Looking over the laboratory grades
the author noted two students had achieved scores of only 50 percent
on the “Physical Properties of DNA“. This was a very low score
compared with the others. As mentioned previously, the post test.on
carbohydrates was not very positive primarily due to student apathy,

but objectives were met as evidenced by the regular test scores.

CONCLUSIONS AND REFLECTIONS

Wt:

Undoubtedly, the major highlight of the unit for the students and
the author is the opportunity to work with the current laboratory
procedures. The DNA Fingerprinting article, the Restriction Mapping
article and the subsequent Electrophoresis demonstration was an
effective way to start the unit: this combination truly piqued student
interest. The discussion of DNA Fingerprinting as permissible
courtroom evidence gave students an opportunity to consider a science
based societal issue. The saccharide lab gave students five
consecutive days In the laboratory, giving them a sense of how three
to four continuous hours in a college lab would ‘feel’. The classwork
assignment ‘Looking at the Saccharides in Our Foods’ gave the students
the opportunity to make informed decisions about nutritional content.
The oral report on steroid abuse allowed students a chance to do a
brief literature survey and obtain valuable information on a major
societal issue. Data analysis was the primary objective of many labs
encouraging students to use ‘critical thinking’ procedures. The
demonstrations on Gel Permeation Chromatography and Partition
Chromatography were well recieved and discussed at length. The entire
class period spent looking through the special visuals of 9:11
Ultnastnugtune was ‘fun’ for all and the time passed quickly. The
extra materials in the form of overheads and visuals during review
sessions led to many interesting student observations and questions,
lending valuable connections for students.

46

4?

WWW

The strengths inherent in this unit are many. Students were
required to draw and label the basic structures of compounds in all
sections, not just ‘memorize to recognize’. This technique led to
better understanding and comprehension. The more written biochemical
exercises required of students, the higher the attainment of
objectives. Group work - having students create their own review
assignments, questions and problems - proved to be very beneficial.
Students adapted well to new laboratory techniques. Even though a
mastery level was not achieved by all, the opportunity was available.
The laboratory requirement of 40 percent is believed unique in the
secondary setting and is clearly one of the strengths of this unit.
The assigning of work In small groups showed evidence of this
technique being very helpful, especially for the ‘slower’ learner.
Peer feedback and assistance helps increase comprehension for
students. Emphasis on discussion was to involve all students: the
author believes this emphasis provides a strong teaching methodology
in this unit.

The unit has some weaknesses. One weakness of the unit is the
complete lack of audio-visual materials. Films, videos, and
filmstrips exist, but are not readily available. These audio-visual
materials are unavailable in either the high school library, the
science department library, or the intermediate school district
library. Audiovisuals for biochemistry are available, but are costly.
Another negative aspect of the unit is the lack of ‘hands-on’ models

for students. While the high school science department does have

463

molecular construction models, there is a need to purchase nucleic
acid and other biochemical models. Available time constraint is a
third weakness of the unit. There is not enough time to cover the
objectives in as much detail as the author would prefer. There is
certainly enough biochemical information available to fill an entire
semester. However, in establishing the Chemistry II course the author
was responsible for creating a comprehensive course. For example: the
biochemistry unit was shortened by two weeks in ’90 to include a four
week unit on Environmental Chemistry. Other units were condensed as
well. Another more subtle fault is the one-hour laboratory time
frame. This breaks up the continuity of lab exercises and creates
difficulty in finding an appropriate place to ‘stop’ until tomorrow.
While not a true fault of the unit - but nevertheless a problem - is
the fact that students were not enthusiastic with the pre test and
post test: but most complied well and results on the whole are
accurate.

The evidence presented by the post test scores and the additional
regular test scores is indicative of better student understanding in
biochemistry. Average post test scores - based on mean scores - over
the four sections in ’89 of 75 percent, post test averages (3) of 79
percent in ’90 (not including carbohydrates due to validity concerns)
certainly lend credence that learning has been achieved. Supported by
average regular test scores - again inclusive of all four sections (77
percent in both ’89 and ’90) - evidence is clear that the objectives

were attained, and at nearly the accepted ‘ideal’ value of 80 percent.

49

We

One revision is to create 20 item pre tests and post tests to be
used in all four sections. This would improve the validity of the
test and make subsequent analysis much easier. Secondly more
laboratory objectives should be included. The pre tests and post
tests should be checked to see if they are a true cross sampling.
Distractors for all tests questions need to be reviewed and
improvements made.

The carbohydrate unit needs improvement in two areas: first, to
include more written exercises and second, to incorporate more small
group work. Having students keep a daily or weekly journal including
brief comments concerning content and methods - to be read by the
Instructor - would aid in evaluating and improving the unit. The use
of appropriate hands-on models would aid all students, especially the
visual learners. Field trips to biotechnology industries and/or
university laboratory facilities would give students an oppurtunlty to
see the application of these ‘real world’ techniques. Finally, the
author would bring in as many quality audiovisual materials as

possible in fitting the time frame of the course.

Wm

Additional units that could be included are: Photosynthesis,
Physical Chemistry, Cellular Biochemistry, and a Research Project.
The photosynthesis unit would emphasize: photosystems, the Dark
reaction(s), and plant metabolism. Physical Chemistry’s emphasis

might include: reaction energies and kinetics, chemical equilibrium,

50

and a more in-depth study of oxidation-reduction reactions. A
Cellular Biochemistry unit should consider: anatomy and physiology,
molecular components, transport systems, biosynthesis, and catabollsm
and metabolism. The research project might become the priority unit
of the four. One week of library research, six to eight weeks of
written and oral preparation, and one week for oral reports would work
nicely. The six to eight weeks bf preparation would be done outside
the classroom. How and where high school educators can sqeeze In the

additional weeks necessary for just one unit is the challenge.

GLOSSARY

Alcohol A compound containing a hydrocarbon group and one or more
hydroxyl (-OH) groups.

Alpha amino acids The basic building blocks of proteins: containing
at least one acidic carboxyl group (-COOH) and one basic amino
(-NH2) group on the (alpha) carbon next to the carboxyl group.

Antibody Proteins in the blood that combine with foreign particles
to neutralize them, thus producing immunity.

Anticodons An exposed triplet base found on tRNA that determines
what amino acid to pick up and where to bind on mRNA.

Biochemistry The study of the structure and composition of compounds
that make up the molecular basis of life.

Biosynthesis The building of organic coumpounds by living organisms.

Carbohydrates An organic compound made of C, H, and 0, including
sugars (energy), starch (storage), and cellulose (structure).
The H to 0 ratio is 2:1.

Carbonyl group The structural group containing an oxygen atom double
bonded to a carbon atom in a carbon chain. Example - RCOR’
(keytones).

Catalyst A substance that speeds up the rate of a reaction without
becoming chemically altered or consumed by the reaction.

Cellulose A polysaccharide forming the strong fibrous stucture in
plant cell walls: commonly refered to as roughage or fiber.

Chitin A polysaccharide that is the major component of the
exoskeleton of crustaceans and insects. It also makes up the
cell wall of fungi.

Cholesterol A lipid which is the metabolic precursor for the five
major classes of steroid hormones containing the ‘backbone’
structure - three cyclohexane rings and one cyclopentane ring.

Codons A group of three nucleotides found on mRNA that code for a
specific amino acid

Coenzyme Specific cofactors that are complex nonproteln organic
molecules that act with enzymes in catalyzing reactions.
Example - vitamins

Cofactor The prosthetic group of a conjugated enzyme that is
necessary for the enzyme to function properly.

51

52

Conjugated enzyme An enzyme that has a prosthetic group attached.

Conjugated proteins Proteins that, when hydrolyZed, yield amino
acids and other organic or inorganic components.

Dehydration synthesis The formation of complex organic molecules
involving the removal of a molecule(s) of water.

Denaturation The loss of the characteristic biological activity of
proteins due to any of a variety of extremes.

Digestion The process by which foods are broken down into small,
water-soluble molecules.

Disaccharide The sugar formed by the chemical combination of two
simple sugars (monosaccharides). Example - sucrose.

DNA (deoxyribonucleic acid) A molecule consisting of alternating
five carbon sugar units (deoxyribose) and phosphate molecules
connected by specific nitrogenous bases. This is a double-helical
structure which contains the genetic code.

Enzyme A protein catalyst produced by the cell for the purpose of
speeding up specific organic reactions at body temperatures.

Essential amino acids The amino acids that must be ingested because
higher animals cannot synthesize them.

Ester The compound formed by the reaction between an alcohol and an
acid.

Fats Esters of glycerol and three different (mostly saturated) fatty
acids: are solids at room temperature.

Fatty acids Carboxylic acids with long, even-numbered carbon chains.

Glycerol An alcohol with three hydroxyl groups on three carbon
atoms; also called glycerin. Has the chemical formula C3H5(0H)3.

Glycogen The readily available storage form of glucose that is
stored in the liver and skeletal muscle.

Hommone Biological regulators that are secreted by glands or organs
that control chemical reactions in other parts of the body.

Hydrogen bonding A weak chemical bond between hydrogen on one polar
molecule and a highly electronegative atom on another molecule.
Most commonly found in water molecules. '

Hydrolysis The chemical breakdown of a substance by the addition of
a water molecule.

53

Hydrophillc The polar head group of a phosphollpid or glycolipld
that has an affinity for water In the membrane lipid bilayer.

Hydrophobic The hydrocarbon tail of a phosphollpid or glycolipld
that avoids water molecules thus forming the nonpolar interior of
the lipid bylayer

Hydroxyl group Has the symbol -OH which covalently bonds to alkanes
to form alcohols. Not to be confused with the hydroxide (OH‘)
ion.

Lipids Several classes of organic compounds composed of C, H, and O
which are insoluble in water. Formed from fatty acids and
alcohols these have a H to 0 ratio greater than 2:1. Examples -
fats, waxes, and steroids.

Metabolism The highly Integrated network of chemical reactions that
enables cells (organisms) to obtain energy and synthesize
molecules.

Monosaccharide The simple sugars: these carbohydrates cannot be
broken down into simpler carbohydrates. Example - glucose.

mRNA (messenger RNA) A single stranded polynucleotide that carries
the genetic code from the nucleus (after transcription) to the
ribosomes.

Neutral lipids Commonly known as fats and oils, these compounds are
esters of glycerol and three fatty acids.

Nucleic acids Polynucleotides that are responsible for making
proteins (RNA) and and passing on genetic information (DNA).

Nucleosides Basic building block of nucleic acids composed of a
sugar and a nitrogenous base.

Nucleotides A nucleoside that has a phosphate group attached after
reacting with phosphoric acid. Thus it is composed of a
nitrogenous base, a five carbon sugar, and phosphoric acid.

Oil A neutral lipid that is a liquid ester of glycerol and virtually
unsaturated fatty acids.

Oligosaccharides Complex sugars containing two to ten
monosaccharides most of which are disaccharides.

Organic modecules Compounds containing carbon that are essential to
- or produced by - living organisms, excluding C0, C02. and
carbonates.

Pectin Polymers of saccharides found in many fruits and plant cell
walls.

54

Peptides Joined amino acids resulting from the process of
dehydration synthesis. Two amino acids - dipeptide.

Phospholiplds A class of lipids composed of glycerol, two fatty
acids, and a phosphate group.

Polypeptides One step below a protein, made up of up to fifty amino
acid subunits linked by peptide bonds.

Polysaccharlde Carbohydrates that are very long, straight or

branched chains composed of up to thousands of monosaccharide
units.

Prosthetic group The nonanino acid part of a conjugated protein.

Protein Organic molecules that contain C, H, O, and N: that are
complex chains of amino acids essential for nearly all aspects of
cellular structure and function.

Regulator Compounds in the body that serve to control or direct a
multitude of physiological functions. Example - hormones.

Replication A process that occurs only in the nucleus where a DNA
molecule duplicates an exact copy of itself.

RNA (ribonucleic acid) A single stranded nucleic acid, containing
the sugar ribose, found primarily in the cytoplasm that carries
out protein synthesis.

rRNA (ribosomal RNA) Serves an important role In translation as the
bonding site to mRNA and moves along the mRNA as tRNA puts the
amino acids in proper sequence.

Simple enzymes Yield only amino acids when hydrolyzed: does not
contain any cofactors.

Simple proteins Yield only amino acids when hydrolyzed: contain no
prosthetic groups whatsoever.

Starch Polysaccharldes that are composed of polymerized glucose
units that are the most important source of dietary carbohydrates
(stored energy).

Steroids Composed of three fused cyclohexane rings and one
cyclopentane ring: these are Important biological regulators
which can cause dramatic physiological effects.

Substrate The reactant substances that the enzymes attach to and act
upon In enzyme catalyzed reactions.

Transcription The process by which DNA makes mRNA to transfer
information for protein synthesis.

55

Translation The process carried out by all three forms of RNA and
ribosomes to bond amino acids in a specific sequnce to form
proteins.

tRNA (transfer RNA) Shaped like a cloverleaf, this molecule has an
anticodon that determines which amino acid to pick up and which
codon to bind to on the mRNA: ‘the workhorse of translation’.

Waxes Large esters of long chain fatty acids and monohydroxyl
alcohols that form protective, waterproof coatings on the
surfaces of leaves and fruits for plants and on skin, fur, and
feathers for animals.

APPENDI CES

APPENDIX A

II.

APPENDIX A

OUTLINE FOR CHEMISTRY II

Inorganic review (time: 2-3 wks)

A.

Nomenclature
1. Naming elements, ions, and compounds
2. Empirical and molecular formulas

. Writing and balancing formulas and equations
. Stoichiometry

1. Percent composition
2. Mass to mass

3. Gas laws

4. Molality and molarity
Solutions

1. Solubility

. Ionization

1. Electrolytes
2. Nonelectrolytes

. Acids, bases, and salts

1. Definitions
2. Properties
3. Indicators

Titration, pH and Buffers (3-4 wks)

A.
B.

C.

D.

Equivalents
1. Normality
pH
1. Ion concentration in water
2. Calculations
3. Neutralization reactions
Titrations
1. Molar solutions
2. Normal solutions
3. Indicators
4. pH measurement
Buffers
1. Definition
a. Function
2. Preparation
a. Properties and components
b. Henderson-Hasselbach equation
c. Titration principles
3. Physiological importance
a. Homeostasis
(1). cellular level
(2). systems
(a) blood

56

57

(3). organisms
(4). ecosystems
(a). acid rain

III. Organic chemistry
A. Carbon coumpounds
1. Oxides
2. Bonding
3. Structures
8. Hydrocarbons
1. Structural formulas
2. Nomenclature
3. Petroleum products
a. Separation techniques
C. Hydrocarbon Substitution products
1. Alkyl Halides
a. Freon type compounds
b. Structures
2. Alcohols
a. Preparation
b. Reactions
. Ethers
. Aldehydes
Keytones
. Carboxylic Acids and Esters
a. Preparations
b. Reactions
c. Saponificatlon

GUI-E50)

VI. Biochemistry (9-12 wks)
A. Introduction
1. Definition
a. Biosynthesis
2. Organic molecules
a. Essential chemical elements of life
b. Compounds of living matter
(1). carbon chains
c. Four main classes
(1). carbohydrates
(2). lipids
(3). proteins and enzymes
(4). nucleic acids
8. Carbohydrates
1. Composition and function
a. C, H, and O H:O is 2:1
(1). empirical formula C.(H20)y
b. Energy source
(1). 4 calories per gram
c. Energy store
d. Carbon source
e. Cellular structural material

58

2. Definition
a. Two or more hydroxyl groups and a carbonyl group
b. Three main classes
3. Monosaccharides
a. Simple sugars
(1). the five most common
b. Structure
(1). open chain and ring forms
(2). hydrolysis
c. Nomenclature
4. Disaccharides
a. Double sugars
b. Natural occuring
(1). commercial food sources
c. Structure and composition
(1). CI2H22011 + H20
d. Important disaccharides
(1). sucrose
(2). maltose
(3). lactose
5. Oligosaccharides
a. Two to ten monosaccharides
b. Disaccharides or double sugars
(1). composition
(2). dehydration synthesis
6. Polysaccharldes
a. Five hundred to many thousand monosaccharides
b. Storage and structural
c. Important polysaccharides
(1). starch '
(a). dietary carbohydrate source
(b). stored form in plants
(c). composition
(2). glycogen
(a). stored form in animals
(b). immediate energy source
(3). cellulose
(a). most abundant organic coumpound
(b). plant structures
(c). non-food for humans (FIBER)
(4). pectin
(a). fruits and plant cell walls
(5). chitin
(a). exoskeletons, insects and crustaceans
(b). cell walls of fungi
C. Lipids
1. Composition and function
a. C, H, and O H:O is > 2:1
(1). water-insoluble molecules
(2). building blocks are:

59

(a). fatty acids
(b). alcohols
(c). other substances
b. Major energy store
(1). 9 calories per gram
c. Structural material in membranes
d. Biological regulators
e. Protective components in
(1). bacterial and plant cell walls
(2). insect exoskeletons
(3). coverings of vertebrates
f. Four main classes
. Neutral lipids (triglycerides)
a. Commonly called fats and oils
(1). the “food“ lipids
(2). fats are solid at room temp and oils are liquid
(3). chemical difference
(a). fats - mostly saturated
(b). oils - mostly unsaturated
(c). hydrogenation will solidify oils
b. Function
(1). storage of energy in both plants and animals
(2). other functions in animals
(a). insulation to prevent heat loss
(b). protection against bruises and shock
(c). support for organs in the body
c. Structure
(1). fatty acid esters of the alcohol glycerol
(a). glycerol and three different fatty acids

. Phospholiplds

a. Function

(1). structural elements of cell membranes
b. Structure

(1). glycerol, two fatty acids, and a phosphate group
c. Lecithin

. Waxes

a. Function
(1). protection and waterproofing
(a). leaves, fruit, skin, fur and feathers
(b). beeswax and whale oil
b. Structure
(1). esters of long chain fatty acids & monohydroxyl
alcohols

. Steroids

a. Function
(1). important biological regulators
(2). have dramatic physiological effects
b. Structure
(1). three fused cyclohexane rings and a cyclopentane
ring
c. Examples
(1). cholesterol, hormones, bile, poisons, and vitamin D

60

D. Proteins

1.

Composition and function
a. C, H, O, and N (most also contain sulfur)
(1). some may also contain P, Fe, Zn, and Cu
b. Basic building blocks are alpha-amino acids
c. Energy source
(1). 3.8 calories per gram
d. Most abundant organic compounds within living cells
e. Control cell structure and function
(1). the means by which genetic information is expressed
f. Diverse functions
(1). catalyst and regulators
(a). enzymes and hormones
(2). structural support
(a). bones and cartilage
(3). movement
(a). muscles and tendons
(4). protection
(a). skin and hair
(b). antibodies
(5). transport materials
(a). oxygen by hemoglobin
(6). source of essential amino acids
(7). blood clotting
(a). fibrinogen and thrombin
(8). storage
(a). seed proteins and casein
(9). can be harmful
(a). viruses are mainly protein
(b). snake venom
(c). botulism (bacterial protein)
9. High molecular weight
(1). 6,000 to many million

. Amino acids

a. Contain a carboxyl group and an amino group
(1). general formula
(2). alpha-amino acid
b. Alpha-amino acid
c. Average molecular weight of 120
d. Twenty common amino acids
(1). nomenclature
(2). essential amino acids
Peptides
a. Peptide bonds
b. Dehydration synthesis
c. Tripeptides
Polypeptides
a. 4 to 50 amino acids
(1). over 50, polymers are called proteins
Protein molecule characteristics
a. Each has a specific chemical composition
(1). what amino acids compose it

61

b. How much of each amino acid
c. Order of amino acid arrangement
d. A definite molecular weight
6. Two main classes
a. simple proteins
(1). yield only amino acids when hydrolyzed
b. conjugated proteins
(1). yield amino acids and organic or inorganic
components
(a). when hydrolyzed
(2). prosthetic group
(a). nonamino acid part
7. Common test for protein
a. Biuret reaction
b. Xanthoproteic reaction
8. Other protein properties
a. Hydrolysis
(1). strong acid or base at their boiling point
(2). digestive enzymes at lower temperatures
(a). both yield peptides then amino acids
b. Denaturation
(1). loss of biological activity
(2). caused by
(a). extreme pH or temp
(b). certain chemicals: Pb, Hg, alcohol, or acetone
9. Protein metabolism
a. 20g/day minimum
b. Free amino acid pool
(1). protein turnover
10. Protein digestion
a. Hydrolysis of peptide bonds
b. Enzyme catalyzed
(1). proteases or proteolytic
11. Amino acid biosynthesis
a. Plants
(1). can make all 20 essential amino acids
b. Bacteria
b. Animals
E. Enzymes
1. Are proteins
2. Catalyst
a. Review definition
b. Usually end in -ase
4. Two main classes
a. Simple enzymes
b. Conjugated enzymes
(1). prosthetic group
(2). cofactors and coenzymes
5. Biochemical reactions
a. Enzyme substrate complex
(1). specific sites
(2). lock and key

b.

_c.
d.

62

Digestion
(1). amylase - starch
(a). mouth
(2). lipase - fats or oils
(a). small intestine
(3). pepsin - proteins
(a). stomach
(4). trypsin - proteins
(a). small intestines
(5). peptidase - polypeptides
(a). small intestine
Metabolism
Synthesis of proteins
(1). amino acids ---> polypeptides ---> proteins
(2). two step process

6. Factors affecting reactions

a.

b.
c.
d.

Concentration of enzyme

(1). I 1 denotes concentration
Concentration of substrate

pH

Temperature

F. Nucleic acids
1. Cellular structure review
2. Two main functions

a. Making proteins

3.

b.

Passing on genetic information

Scientific contributions
a. Watson and Crick

b.
. Chemical nature

Franklin

a. Basic building blocks

b.

d.

(1). nucleotides

Molecular weights

(1). DNA - ten billion range

(2). RNA - twenty five thousand range

. Composition

(1). nucleotides
(a). pyrimidines and purines
(b). base pairing of DNA and RNA

(2). five carbon sugar

(3). phosphoric acid

(4). nucleosides

Reactions

(1). formation of DNA

(2). formation of RNA

(3). role of ADP and ATP

5. DNA

a.

Genetic information
(1). replication

(2). hydrogen bonding
(3). amino acid pairing

V.

VI.

VII.

63

6. RNA
a. Three types
(1). mRNA. rRNA, and tRNA
b. Protein synthesis
(1). five step process
(2). transcription - first step
(a). nucleus
(3). translation - four step process
(a). cytoplasm
(b). function of mRNA, rRNA, and tRNA
(c). peptide bonds
(d). codons and antlcodons
7. Amino acids
a. abbreviations
8. Comparison of DNA and RNA

Photosynthesis (2-3 wks)
A. Photosystems

B. Dark reactions

C. Metabolism

Projects (2 wks)
A. One week library research

1. Six to eight weeks to put project together
B. One week for presentations

Physical chemistry
A. Reaction energy and kinetics
1. Units and symbols
2. Heat of formation
3. Exothermic and endothermic reactions
4. Factors influencing reactions
B. Chemical equilibrium
1. Reversibility
2. Constants
3. Solubility
C. Oxidation-reduction
1. Electrochemistry
2. Electroplating

VIII. Environmental Chemistry

A. Geology and geography of the Great Lakes
1. Formation
2. Water flow
a. Great Lakes basin
b. watershed
c. wetlands
d. fresh water
B. The water cycle
1. Man’s Influenee
C. Abiotic and biotic factors
1. Physical properties

64

a. pH
b. dissolved oxygen (0.0.)
c. hardness
d. concentration of carbon dioxide [C02]
e. temperature
2. Flora and fauna
D. Energy relationships and interactions
1. Ecosystem
a. niche
b. habitat
c. pyramid of energy
(1). food chain
2. Photosynthesis and respiration
3. Cycles
a. carbon
b. nitrogen
c. phosphorus
4. Energy flow
1. lake ecosystem
2. stream ecosystem
E. Man’s impact on the Great Lakes
1. Positive and negative impacts
a. use and abuse
b. effects on groundwater
2. Industrial and agricultural use
3. Regulation
4. Economic importance
a. five major areas
5. Who should control the Great Lakes
a. ‘who pays to play’

IX. Additional units if time permits
A. Cellular biochemistry
B. Research projects

APPENDIX B

APPENDIX B

Daily Journal

Day - 1 Monday: 2-12-90

LESSON PLAN -

Introduction to Biochemistry

Pre-Test: Carbohydrates (appendix D)

Assignment: Read worksheet #1 - ‘The Chemistry of Living
Things’

Review: Buffers and their physiological importance

- (appendix A)

Lecture notes and discussion: see outline (appendix A)
Teaching assists - overhead projector, blackboard, &
visuals (appendix H)

Homework: Questions 1-9 worksheet 1

Day - 2 Tuesday: 2-13-90

LESSON PLAN

Correct homework and discuss

Finish lecture

Homework: Handout “Long Arm Of The Lab“ - DNA
Fingerprinting Article from Ibe_flgt;glt_£nee_£ness
Students are to read, summarize and include their
opinion of this ‘state of the art technique’ as
permitted by the courts to use as evidence.

Day - 3 Wednesday: 2-14-90
LESSON PLAN

Collect DNA Fingerprinting summary

Discussion: article itself, grading procedure - content,
grammar, spelling, punctuation, and clarity.

Demonstration: How gel electrOphoresls works

Handout: “Construction of a RestriCtion Map of the
Bacteriophage Lambda“ - article on electrophoresis by
Dr. Clarence Suelter, M.S.U.

Homework: Worksheet #2 ‘Carbohydrates’ read for tomorrow.

Day - 4 Tuesday: 2-20-90 (2-15 snow day: 2-16 thru 2-19 mid-winter
recess)

LESSON PLAN

Return summary of ‘DNA’ article
Discussion: restriction mapping article and

65

66

electrophoresis demonstration
Lecture and notes on carbohydrates: see outline
- (appendix A)
Teaching assist - overhead projector, blackboard and
visuals (appendix H)
Homework: Draw and determine the differences of
monosaccharides.

Day - 5 Wednesday: 2-21-90

LESSON PLAN
Correct and discuss homework
Continue with notes on carbohydrates
Homework: Draw the structure and know the composition of
sucrose, maltose, and lactose

Day - 6 Thursday: 2-22-90

LESSON PLAN
Correct and discuss disaccharlde homework
Finish notes
Demonstration: cellulose Is fiber - wheat, grass,
cattails, rope, cereal, lettuce etc.
Homework: Questions 1-10, Worksheet 2

Day - 7 Friday: 2-23-90

LESSON PLAN
Correct homework
Classwork: complete pre-lab worksheet (appendix G)
Correct and discuss in class
Handout Saccharlde Lab - four sections
Homework: Read information on Benedict’s test In lab
handout

Day - 8 Monday: 2-26-90

LESSON PLAN
Lab: Benedict’s Test - part 1
Homework: Read Iodine test procedure

Day - 9 Tuesday: 2-27-90

LESSON PLAN
Lab: Iodine test - part 2
Homework: Read procedure for Acid Hydrolysis of
Saccharides

Day - 10 Hednesday: 2-28-90

LESSON PLAN
No class: National Honor Society meeting

Day

Day

Day

Day

Day

Day

Day

67

11 Thursday: 3-1-90

LESSON PLAN
Lab: Acid Hydrolysis - part 3
Homework: Read Enzymatic Hydrolysis of Saccharides:
Amylase Action on Starch

12 Friday: 3-2-90

LESSON PLAN
Lab: Enzymatic Hydrolysis - part 4

13 Monday: 3-5-90

LESSON PLAN
Finish Enzymatic Hydrolysis lab analysis and questions for
the previous labs. Hand in completed Saccharide lab.
Homework: Bring in at least three food labels that have
the nutritional (carbohydrate) content listed.
Cereal packages are recommended.

14 Tuesday: 3-6-90

LESSON PLAN
Hand back and discuss Saccaharlde lab
Classwork: ‘Looklng At The Saccharides In Our Foods’
- (appendix G)
Homework: Study for carbohydrate quiz tomorrow. Test on
Friday.

15 Wednesday: 3-7-90

LESSON PLAN
Hand back and discuss Saccharides in our Foods.
Take last minute questions before quiz.
Adninlster quiz. (appendix E)

16 Thursday: 3-8-90

LESSON PLAN
Correct Quiz and discuss.
Review: Carbohydrates - emphasis on lab work
Teaching assists - overhead and blackboard (appendix H)

17 Friday: 3-9-90

LESSON PLAN
Release day for Science Olympiad Team.
Other class members (6) aid in setting up events.
No assignment

Day

Day

Day

Day

Day

Day

Day

68

18 Monday: 3-12-90

LESSON PLAN
Use overheads from ‘Blochemlstry 200’ illustrations to
review stuctures emphasized in previous labs.
- (appendix H)
Hand out salivary amylase lab and give background
information In pre lab disscussion.
Homework: Read lab, pay close attention to procedure.

19 Tuesday: 3-13-90

LESSON PLAN
Lab: ‘General Effect of Salivary Amylase 0n Starch’

20 Wednesday: 3-14-90

LESSON PLAN
Lab: finish ‘Salivary Amylase lab’
Homework: Complete lab write-up and data analysis
Carbohydrate test on Friday 3-16

21 Thursday: 3-15-90

LESSON PLAN (Guest Teacher - ‘Substitute’)
Collect labs
Students are to work in groups and study for tomorrow’s
test. Develop questions and answers then exchange
between groups. Have guest teacher collect.
Reminder: Test tomorrow

22 Friday: 3-16-90
LESSON PLAN A

Adninister Carbohydrate Test (appendix F)

Handout: Pick-up lipid worksheet

Homework: Read pages 10-11 of Lipid Worksheet #3 for
Monday.

23 Monday: 3-19-90

LESSON PLAN
Post Test: Carbohydrates (appendix D)
Correct regular test and discuss.
Hand back labs and discuss.
Homework: Finish reading Lipid Worksheet #3 for Wednesday.

24 Tuesday: 3-20-90

LESSON PLAN
No class: Drama Club Play

69

Day - 25 Wednesday: 3-21-90

LESSON PLAN

Pre-Test: Lipids (appendix D)

Lecture notes and Discussion: see outline (appendix A)
Teaching assist - overheads, blackboard and visuals
- (appendix H)

Homework: Questions 1-10 end of lipid worksheet, due

tomorrow.

Oral report on steroid abuse due Monday 3-26.
Students are to do a literary survey finding
information on an athlete who has used/abused
steroids and report results. (appendix G)
Read Spec 20 lab for tomorrow.

Day 26 Thursday: 3-22-90

LESSON PLAN
Lab: ‘Introduction To Spectrophotometry’

Day - 27 Friday: 3-23-90
LESSON PLAN
Lab: finish Spec 20 lab
Homework: Complete lab write-up and data analysis.
Reminder: Oral report on steroids due Monday.
Day - 28 Monday: 3-26-90
LESSON PLAN
Hand back homework from lipid worksheet and discuss.
Oral reports on steroids
Collect Spec 20 labs
Homework: Read fat digestion lab for tomorrow.
Day - 29 Tuesday: 3-27-90
LESSON PLAN
Lab: Fat Digestion (appendix I)
Homework: Lab write-up and data analysis
Day - 30 Wednesday: 3-28-90

LESSON PLAN
Collect labs and discuss
Lecture: finish notes on lipids
Teaching assists - overheads from ‘Biochemlstry 200’
and Wm
- (appendix H)
Homework: Test Friday on Lipids

70

Day - 31 Thursday: 3-29-90

LESSON PLAN
Review for test on lipids tomorrow. Whole class, then
small groups.

Day - 32 Friday: 3-30-90

LESSON PLAN
Administer Test on Lipids (appendix F)
Post test: Lipids (appendix D)

Day - 33 Monday: 4-9-90

LESSON PLAN
Hand back fat digestion lab
Return regular lipid test and discuss
Pre-test: Proteins & Enzymes (appendix D)
Hand out Protein workSheet
Home work: Read all of Protein Worksheet #4 and answer
questions 1-10 for tomorrow.

Day - 34 Tuesday: 4-10-90

LESSON PLAN
Correct homework and collect
Lecture and discussion notes on proteins: see outline
- (appendix A)
Teaching assists - overheads, blackboard, and visuals
- (appendix H)
Handout Enzyme worksheet
Homework: Read all of Enzyme Worksheet #6.

Day - 35 Wednesday: 4—11-90

LESSON PLAN

Oral quiz on reading assignment

Finish notes on proteins and complete enzyme lecture as
well.
Teaching assists - overheads, blackboard, and visuals

- (appendix H)

Homework: Do questions 1-10 on enzyme worksheet for

tomorrow.

Day - 36 Thursday: 4-12-90

LESSON PLAN
Wrap up enzyme notes.
Correct enzyme homework and discuss.
Students help set up lab for tomorrow.

71

Homework: Read ‘Qualltative Analysis of Proteins and Amino
Acids’ for Friday: we’ll do part one of three
tomorrow.

Day - 37 Friday: 4-13-90

LESSON PLAN .
Demonstration: Partition Chromatography and determination
of R; values
Lab: ‘Qualitative Analysis of Proteins and Amino Acids’ -
part I Ninhydrin test
Handout: Read Stryer’s discussion of enzyme-substrate
complexes.

Day - 38 Monday: 4-16-90

LESSON PLAN
Discussion of Partition Chromatography
Lab: Finish parts 11 and III, Biuret’s and Xanthroproteic
test for Qual. Anal. of Proteins

Homework: Study for quiz tomorrow over proteins and
enzymes.

Day - 39 Tuesday: 4-17-90

LESSON PLAN
Classwork: Students are to share all lab data on overhead
for analysis and discuss. Then determine unknown on
their own and turn In lab.
Discuss Stryer’s enzyme handout.
Quiz: Proteins and Enzymes (appendix E)

Day - 40 Wednesday: 4-18-90

LESSON PLAN

Correct quiz and discuss.

Review: protein structures (primary thru quaternary),
enzymes, dehydration, hydrolysis, denaturation etc.
Use overheads from ‘Biochemistry 200’, flapng;§
3.122113111151112. and W
as well as visuals.

- (appendix H)

Homework: Read ‘Protein Digestion By Papain & Bromelain’

for lab tomorrow.

Day - 41 Thursday: 4-19-90

LESSON PLAN
Lab: ‘Protein Digestion By Papain a Bromelain’ Do set-ups
1-3 to prepare for tomorrow.
Demonstation: Gel Permeation Chromatography
- (appendix I)
Homework: Re-read procedure for taking readings and change
time to 5 minutes.

72

Test on Monday over Proteins and Enzymes.
Day - 42 Friday: 4-20-90

LESSON PLAN
Lab: Check and adjust pH of enzyme solutions. Run lab and
take readings every 5 minutes.

Homework: Lab write-up and data analysis are due Monday.
Reminder: Test Monday

Day - 43 Monday: 4-23-90

LESSON PLAN
Collect labs
Administer Test on Proteins and Enzymes (appendix F)
Post Test: Proteins and Enzymes (appendix D)
Handout: Nucleic Acid Worksheet

Homework: Read first two pages of Nucleic Acids Worksheet
#5.

Day - 44 Tuesday: 4-24-90

LESSON PLAN
Hand back regular test and discuss.
Pre-test: Nucleic Acids (appendix D)
Lecture notes and discussion on Nucleic Acids: see outline
- (appendix A)

Teaching assists - overheads, blackboard, and visuals
- (appendix H)

Homework: Read remainder of worksheet on nucleic acids.
Day - 45 Wednesday: 4-25-90

LESSON PLAN

Hand back protein digestion lab and discuss.

Classwork: Read Chpt 7 in Mgggnn_fliolggy - ‘Nucleic Acids
and Protein Synthesis’ pgs 100 thru 111.
Continue notes on nucleic acids.
Teaching assists - overheads from Modern_hlglggy,
‘Schaum’s Outline Series’ and ‘Biochemistry 200’
- (appendix H)

Homework: Review all steps in protein synthesis.

Day - 46 Thursday: 4-26-90

LESSON PLAN
Finish lecture notes
Review: sequencing, replication, transcription, protein
structures, and translation. Use overheads from
Nucleic Acid Worksheet and ‘Biochemlstry 200’ also

visuals from £21L_Biglggy (appendix H)
Discussion of above

73

Homework: Do questions for review and applying concepts on

page 112 in Modern_fijglggy for tomorrow.
Day - 47 Friday: 4-27-90

LESSON PLAN
Collect homework
Science Olympiad preparation for State competition
tomorrow.

Day - 48 Monday: 4-30-90

LESSON PLAN
Hand back homework and discuss
Special visuals: 9:11.011rastructure - booklet of electron
and light microscopy of cellular structures and
features. Used to tie all units of Biochemistry
together and bring in examples of biotechnology.
Homework: Questions 1-11 end of worksheet #5.

Day - 49 Tuesday: 5-1-90

LESSON PLAN

Correct homework and discuss

Classwork: Students are to develop sample questions and
problems for all nucleic acid terms from list
provided, include an answer key. (appendix G).

Homework: Students are to exchange developed questions and
problems: answer classmate’s worksheet for tomorrow.
Test on Nucleic Acids on Thursday.

Day - 50 Wednesday: 5-2-90

LESSON PLAN
Collect homework
Lab: ‘Physlcal Properties of DNA’
Collect labs and discuss
Reminder: Test tomorrow

Day - 51 Thursday: 5-3-90

LESSON PLAN
Hand back homework and discuss
Adninister Test on Nucleic Acids (appendix F)

Day - 52 Friday: 5-4-90

LESSON PLAN
Post Test: Nucleic Acids (appendix D)
Correct regular test and discuss

Wm

APPENDIX C

APPENDIX C

BIOCHEMISTRY PRE AND POST INTERVIEW FOR CHEM II

Student’s Initials Age Sex

Grade Overall G.P.A.

 

Educational Background (Schools Attended)

 

Sciences classes (H.S.)

Earth Science Physical Science Biology ____

 

 

Chemistry Physics Anatomy & Physiology ____

 

Other

 

Personal goals:

College Other

 

Major/Minor Career

 

Additional comments concerning your science education.

 

 

Pre-Test and Post Test Interview

What is biochemistry?

 

 

What is biosynthesis?

 

 

74

75

There are four main classes of organic molecules. Name them.

1 2 3

 

4

 

The major use of carbohydrates by living things is for

 

Carbohydrates contain which elements?

 

List the three main classes of carbohydrates. 1

 

2 and 3

 

How does glycogen differ from starch?

 

 

The largest use of lipids by humans is for

 

Triglycerides or neutral lipids are commonly called

 

and

 

A main function of waxes in the living world is for

 

Two common examples of steroids are and

 

Which element is found in proteins but not carbohydrates or

lipids?

 

The basic building blocks of proteins are

 

Define a conjugated protein.

 

 

What Is meant by a denatured protein?

 

 

Enzymes are the catalyst for digestion and in

animals.

76

DNA and RNA are nucleic acids responsible for

and

 

 

respectively.

Define: replication, transcription, and translation.

 

 

 

What are ‘Buffers’?

 

 

List three key areas of physiological importance of buffers.

 

 

 

Why is the study of Biochemistry important to you?

 

 

 

 

Why is the study of Biochemistry Important to mankind?

 

 

 

How do you think this unit will benefit you in your college science

courses?

 

 

 

APPENDIX D

APPENDIX D

CARBOHYDRATES: PRE-TEST AND POST TEST

MULTIPLE CHOICE

1.

10.

11.

Glucose and galactose make up a molecule of (a) sucrose (b)
lactose (c) maltose (d) all of these

A simple sugar consists of (a) an hydroxyaldehyde (b) an acid and
an alcohol (c) an acid and a keytone (d) an hydroxyketone (e)
either a or d

The energy supplied by carbohydrates in calories per gram is (a) 9
(b) 3.8 (c) 4 (d) 6.2

Carbohydrates supply (a) energy (b) carbon (c) cellular structural
material (d) none of these (e) all of these

A sugar that can be found in fruits and honey is (a) fructose (b)
lactose (c) glucose (d) sucrose (e) both a and c

All of the following are true of mono- and disaccharides exggpt(a)
they taste sweet (b) they are white crystalline substances (c)
they are soluble in water (d) they form a red precipitate in

Fehling’s or Benedict’s solutions (e) they are known collectively
as sugars

The process by which a dilute acid breaks down a complex
carbohydrate into simpler ones is known as (a) hydrolysis (b)
biosynthesis (c) dehydration (d) carbonyl grouping

Starch turns dark blue in the presence of iodine because the
iodine reacts with what compound found in the starch molecules (a).
amylase (b) amylose (c) amylopectin (d) lypase (e) none of these

Dehydration synthesis of glucose and fructose produces (a) maltose
(b) lactose (c) pentose (d) sucrose (e) all of these

The structural polysaccharide found in plant cells is (a)
cellulose (b) maltose (c) sucrose (d) lactose (e) deoxyribose

The ‘souring’ of milk, yogurt, and cottage cheese Is produced by

bacteria acting on (a) a polysaccharide (b) cellulose (c) lactose
(d) sucrose (e) maltose

77

12.

13.

14.

15.

OG‘KIO‘UIJLQN"

78

Polysaccharldes are chains of how many monosaccharides (a) two or
more (b) ten or more (c) fifty to on hundred (d) one hundred to
five hundred (e) five hundred to many thousand

Which of the following is not a polysaccharide (a) glycogen (b)
cellulose (c) pectin (d) chitin (e) all are polysaccharides

Animals store saccharides in the form of (a) cellulose (b)
glycogen (c) pectin (d) chitin (e) starch

A carbohydrate that cannot be hydrolyzed is (a) sucrose (b) starch
(c) glycogen (d) fructose (e) all of these

Carbohydrate - Key

QUGQOD‘QUWQGQOGU

LIPIDS: PRE-TEST AND POST TEST

MULTIPLE CHOICE

HQQflO‘O‘IwaH

o.

For lipids the ratio of H to O is (a) 2:1 (b) > 2:1 (c) < 2:1 (d)
3:1

Lipids are (a) a major energy store (b) structural materials in
membranes (c) biological regulators (d) protective components (e)
all of these

Triglycerides are commonly called (a) waxes (b) steroids (c) fats
and oils (d) proteins (e) all of these

The structure of neutral lipids is (a) glycerol and two fatty
acids (b) ethanol and two fatty acids (c) ethanol and three fatty
acids (d) glycerol, ethanol and a fatty acid (e) three fatty acids
and glycerol

The function of phosphollpids Is for (a) insulation (b) structural
elements of cell membranes (c) transfer of electrical impulses (d)
blood clotting (e) none of these

How many classes of lipids are there (a) 5 (b) 4 (c) 3 (d) 2 (e)
1

Lipids form waterproof coatings on all of the following except (a)
eyes (b) leaves (c) feathers (d) fruits (e) skin

An example of a steroid is (a) hormones (b) bile (c) cholesterol
(d) vitamin D (e) all of these

The structure of steroids is made up of (a) three cyclohexane
rings (b) long chain fatty acids (c) glycerol (d) a cyclopentane
ring (e) a and d

. What is the pH of a solution of digested fats (a) > 7 (b) < 7 (c)
7 (d) could be >or< 7 (e) does not change

LIPID KEY

UOGUU’O’GOOU

79

PROTEINS/ENZYMES: PRE-TEST AND POST TEST

MULTIPLE CHOICE

1. The element common to proteins that is not found in carbohydrates
or lipids is (a) H (b) Na (c) K (d) N (e) Ca

2. The basic building blocks for proteins are (a) lipids (b)
carbohydrates (c) hydrocarbons (d) triglycerides (e) amino acids

3. The amount of calories available per gram of protein is (a) 3.8
(b) 9 (c) 4.2 (d) 6 (e) 5.2

4. Proteins are most important for (a) structural support
(b) expressing genetic information (c) antibody formation
(d) storage (e) prdtection

5. Long chain polymers of 50 amino acids or more are commonly
referred to as (a) peptides (b) polypeptides (c) proteins
(d) prosthetic group (e) protease

6. The name given to the amino acids that higher animals need to
Ingest, since animals cannot synthesize them, is (a) necessary
(b) photosynthetic (c) essential (d) peptides (e) ingested

7. Every amino acid contains at least one (a) carboxyl group (b)
alcohol group (c) ethyl group (d) amino group (e) both a and d

8. Amino acids are joined together by (a) dehydration synthesis (b)
hydrogenation (c) hydrogen bonding (d) hydrolysis (e) both a and d

9. The name given to the nonamino acid part of a conjugated protein
is a(n) (a) peptide group (b) amino group (c) carboxyl group
(d) prosthetic group (e) conjugate group

10. Proteins have many diverse functions except (a) being found in
snake venom (b) being the main component in viruses (c) being
found in the bacteria that causes botulism (d) being responsible
for blood clotting (e) being the most abundant organic compound
found in nature

11. Proteins have molecular weights ranging from (a) 6,000 to many
million (b) 100 to 6,000 (c) 600 to 10,000 (d) 1 to 6
(e) 6 million to 100 million

12. The name given to the C-N bond between two amino acids is
(a) alpha bond (b) amide bond (c) peptide bond (d) hydrogen bond
(e) acidic bond

80

13.

14.

15.

16.

17.

18.

19.

20.

81

The test given for proteins that results In a violet color when an
alkaline suspension of a protein is treated with a solution of
copper II sulfate is called (a) BCA assay (b) Hydrolysis

(c) Dehydration (d) Biuret (e) Xanthroprotelc

Proteins exposed to extremes of pH, temperature, and/or chemicals
lose their biological activity. This condition is called

(a) death (b) prosthesis (c) functional inhibition

(d) denaturation (e) constipation

Which of the following chemicals would cause a protein to lose its
characteristic biological activity. (a) alcohol (b) mercury salts
(c) lead salts (d) acetone (e) all of these

The substance that an enzyme causes to react is called the
(a) coenzyme (b) cofactor (c) substrate (d) catalyst (e) complex

The primary function of enzymes is to (a) increase the rate of
reactions (b) aid digestion (c) allow metabolism to take place
(d) create a ‘buffered’ environment (e) break down vitamins

The name given to the prosthetic group of a conjugated enzyme,
necessary for the enzyme to function properly, Is (a) coenzyme
(b) metabolite (c) cofactor (d) active site (e) substrate

All of the following are responsible for the hydrolysis of

proteins except (a) trypsin (b) pepsin (c) peptidase (d) amylase
(e) none of these

The complex reactions that take place in our bodies occur at
relatively low temperatures. The loss of enzyme activity due to a
temperature increase begins at celsius temperatures of

degrees (a) 37 (b) 45 (c) 30 (d) 55 (e) 50

omummawww

UQOO’OQQQOWGQOIGOOU‘OGQ

82

PROTEIN/ENZYME - ANSWER KEY

NUCLEIC ACIDS: PRE-TEST AND POST TEST

MULTIPLE CHOICE

1.

IO.

11.

Which of the following Is not a basic component of a nucleotide?
(a) nitrogenous bases (b) a five carbon sugar (c) acetic acid
(d) phosphoric acid (e) both c and d

Which of the following statements is incorrect? (a) DNA is a
double strand helix, RNA is a single strand (b) the sugar in DNA
is deoxyribose whereas RNA has ribose (c) DNA adenine bonds to
thymine, RNA adenine bonds to uracil (d) DNA is a much bigger
molecule than RNA (e) all of the above are correct

The major portion of which of the following is found outside the
nucleus of the cell? (a) DNA (b) chromosomes (c) RNA (d) nucleolus
(e) none of these

DNA Is produced by which part of the cell? (a) cytoplasm (b)
nuclear membrane (c) plasma membrane (d) ribosomes (e) nucleus

mRNA is produced from DNA by the process known as:
(a) transcription (b) replication (c) ribofraction (d) synthesis
(e) none of these

What is the difference between a nucleic acid and a
polynucleotide? (a) There Is no difference (b) a nucleic acid has
a minimum of three polynucleotides (c) polynucleotides do not have

acids attached (d) nucleic acids have the base removed (e) both c
and d

ADP and ATP are very important for cellular function. Both are
classified as (a) polynucleotides (b) nucleic acids (c) vitamins
(d) mononucleotides (e) proteins

In DNA which bases bond to each other? (a) adenine bonds to
thymine (b) glycine bonds to tryptophan (c) cytosine bonds to
guanin (d) cytidine bonds to isoleucine (e) both a and c

Pyrimidines and purines are commonly referred to as (a) nucleic
acids (b) nitogenous bases (c) sugars (d) amino acids
(e) nucleoside

Which type of RNA does not exist? (a) messenger RNA (b) transfer
RNA (c) ribosomal RNA (d) chromosomal RNA

DNA is responsible for (a) cellular control (b) passing genetic
information (c) energy storage and release (d) synthesizing amino
acids (e) all of these

83

12.

14.

15.

‘OQNGUIJLWNH

O

HHHHHH
mAwNI-‘O

84

Nucleic Acids - cont.

When DNA ‘unzips’ itself this process is known as (a) replication
(b) transcription (c) hydrolysis (d) translation (e) self-
revelation

. RNA is responsible for (a) making ribosomes (b) passing genetic

information (c) protein synthesis (d) monitoring the cytoplasm
(e) all of these

Codons and anticodons are found respectively on (a) cRNA and tRNA
(b) mRNA and rRNA (c) rRNA and tRNA (d) cRNA and rRNA (e) mRNA and
tRNA

Anticodon GCA would match with codon (a) CAU (b) AAU (c) CGU

(d) AGC (e) CUG

NUCLEIC ACID - ANSWER KEY

OOOWUQUOQOOOOQO

APPENDIX E

APPENDIX E

SACCHARIDE OUIZ

CHEMISTRY II NAME

 

1. List the four functions of saccharides. (4 points)

2. Explain what occurs during the Benedict’s test, when testing a
reducing sugar. Describe what happens chemically and to the color
of the solution. (2 points)

3. Explain what occurs during the iodine test, when testing a
branched polysaccharide. Describe what happens chemically and
visually. (2 points)

4. Write the general chemical formula for saccharides. (1 point)

5. Compare and contrast monosaccharides, oligosaccharides, and
polysaccharides. Keep in mind structure and function. (6 pts.)

85

86

SACCHARIDE OUIZ

6. You are to test an unknown sugar: sugar ‘2’. First you test with
Benedict’s and iodine. According to the following data what type

of sugar is sugar 2? Explain how you reached your conclusion.
(5 pts.)

n d' ’ I t II 'ne I u I
Sugar 2 I blue I sneq. (r) II darksblue I pos. (+) I

7. Taking your-original unknown add HCl. After waiting for an hour

you again run the Benedict’s and iodine test. Using the new data
shown below, determine what has happened to sugar 2. Has
hydrolysis occured? Explain. (5 points)

’ I I
Sugar 2 I red. I pos. (+) II yellow .1, neg. (-) I

87
Carbohydrate Quiz - Key

Energy source, Carbon source, Energy storage, and Cellular
material.

The linear sugar reduces the free Cu Ii to Cu I. The solution
changes from blue to red indicating a positive test.

iodine only complexes with helically coiled polysaccharides.
Therefore, it does not complex with brached polysaccharides and

the test yields negative results. The yellow color does not
change.

Mono- 1 sugar quick energy
Oligo- 2-10 sugars energy storage
Poly- > 10 sugars structure and storage

Sugar 2 is a helical polysaccharide. This is indicated by the
positive iodine test. The Benedict’s test is negative which
tells us sugar 2 Is not a monosaccharide.

The positive Benedict’s test indicates that the sugar has indeed
been hydrolyzed. Sugar 2 is no longer a polysaccharide due to
the negative iodine test so we know it has been broken down.

PROTEIN AND ENZYME OUIZ

CHEMISTRY II NAME

10.

 

List three functions of proteins.

In an amino acid where is the alpha carbon located ?

A peptide bond forms between what two atoms (elements) on adjacent
amino acids ?

The chemical process by which amino acids are Joined together is
called ?

The adition of which element distinguishes proteins from
carbohydrates and lipids ?

How many polymers of peptides are necessary to distinguish a
protein from a polypeptide ?

The order in which peptides are put together, (the sequence of
amino acids). has no bearing upon the function of the proteins
they make up. True or False

Protein chains such as hemoglobin are long because if there is an
amino acid substituted or out of place this will have no effect,
due to the lengthy chain. True or False

Simple proteins yield when hydrolized.

Denaturation is caused by ? Give two examples.

88

89

11. Define enzyme.

12. List the four factors that affect enzyme reactions.

13. Describe fully how an enzyme would break down a substrate.

\lO‘UW

(D

10.

11.

12.

i3.

90

PROTEIN QUIZ - KEY

Any three of the following: catalyst & regulators, structural
support, movement, protection, transport oxygen, source of amino
acids, blood clotting, antibodies, compose - viruse, poisons, and
food toxins.

The carbon atom next to the carboxyl group.

Between the nitrogen and carbon atoms.

Dehydration synthesis.

The addition of nitrogen.

Greater than fifty (50).

False

False

amino acids only

Any two of the following: extreme pH, temperature extremes, lead
or mercury salts, acetone, and alcohol.

An enzyme is a protein that acts as a catalyst.
[enzyme], [substrate], pH, and,temperature

The enzyme substrate complex forms like a lock and key. This
takes place at the active site on the enxzyme. The enzyme acts
on the substrate, releases it and the substrate is broken down
into two or more pieces. Ezymes can also act on substrates in a
similar manner to put two substrates together forming one
compound.

APPENDIX F

APPENDIX F

CARBOHYDRATE TEST

CHEMISTRY II NAME

 

CHOOSE THE BEST ANSWER (1 POINT EACH)

1. The sugar ribose is found in a) starch b) chitin c) RNA
d) DNA e) pectin

2. A carbohydrate that cannot be hydrolyzed is a) maltose
b) starch c) lactose d) galactose e) sucrose

3. The sugar that can be found in the exoskeleton of
crustaceans is a) cellulose b) chitin c) pectin d) glucose
e) lactose

4. A molecule of maltose is made up of a) glucose and fructose
b) chitin c) two glucose molecules d) two fructose molecules
e) glucose and galactose

5. Only one of the following is true of polysaccharides:
a) they form a red precipitate with Benedict’s solution
b) they are less than ten monosaccharides

c) they taste sweet

d) they are only used for quick energy

e) they are insoluble in water

6. Pectin is a sugar found as:
a) fruit cell walls

b) plant storage material

c) animal storage material

d) the exoskeleton of insects
e) a water source in fruits

7. The structure shown on the overhead is a simple sugar that
consists of: a) an acid and a ketone b) a base and an aldehyde
c) an hydroxyketone d) an acid and alcohol e) hydroxyaldehyde

8. The ring form that has four carbons and one oxygen making up
the ring is: a) maltose b) furanose c) glucose d) pyranose

e) pentanose

9. The enzyme that breaks down starch is called: a) amylose

b) amylopectin c) starchase d) amylase e) galactose

91

92

FOR THE FOLLWING SECTION. BE AS COMPLETE AND SPECIFIC AS POSSIBLE

10. In the salivary experiment, explain what happened to the starch -
iodine mixture when saliva was added to the tube. Was there a
color change? If so, what color and why or why not? ( 2 pts.)

11. What two forms of starch are there and how do they differ from
one another ? ( 2 pts.)

12. Compare how glucose and sucrose react in the Benedict’s solution.
Explain what type of reaction occurs, the color change involved
and the type of sugar each one is. ( 2 pts.)

13. What did we use as a control for all the saccharide experiments.
What is the control’s Benedict’s reaction ? The control’s iodine
reaction ? Why did you get those results ? ( 3 pts.)

14. For the following sugars, identify whether the sugar is a
monosaccharide, Oligosaccharide, or a polysaccharide; also where
you might find the sugar and its function. (5 pts.)

Sugar Type of sugar Where found Function

Lactose

Galactose

Sucrose

Starch

Fructose

93

15. What is the general formula for all polysaccharides ? ( 1 pt.)

16. What is the chemical formula for maltose and for fructose ?
( 2 pts.)
Maltose Fructose

17. What is the source of fiber for humans ? What type of sugar is
fiber ? < 2 pts.)

FILL IN THE CHART BELOW FOR THE RESULTS OF EACH TEST AND THE TYPE OF
SUGAR. THEN USE THE CHART TO ANSWER THE FOLLOWING QUESTIONS.( 6 pts.)

 

 

Sugar Benedict’s Results Iodine Results Type
A red yellow
B blue yellow
C blue dk blue
D red dk blue
E blue dk blue
F red yellow

 

18. Which sugar(s) are reducing sugars ? Using the above results,
explain your answer. ( 3 pts.)

19. Which sugar(s) are helical polysaccharides ? Explain you answer
according to the results. ( 2 pts.)

20. Which sugar(s) are Oligosaccharides without free aldehyde or
keytone groups ? ( 1 pt.)

21.

94

Compare the type of sugars present in sugars B and D ? ( 2 pts.)

FILL IN THE CHART BELOW FOR THE RESULTS OF EACH TEST AND THE TYPE OF
SUGAR. THEN USE THE CHART TO ANSWER THE FOLLOWING QUESTIONS. ( 9 pts)

22.

23.

24.

25.

 

 

Sugar Benedict’s Results Iodine Results Type
X blue dk blue
X + saliva red yellow
Y blue yellow
Y + HCl red yellow
2 blue dk blue
2 + HCl blue dk blue
W red yellow
V red yellow
W + V blue dk blue

 

What happened when sugars W and V were mixed ? What is the
mechanism of this reaction ? What type of sugars are W and V ?
( 3 pts.)

What happened to sugar X when saliva was added ? Refer to the
type of sugar before and after the reaction. ( 2 pts.)

What happened to sugar Y when HCl was added ? Explain in terms
of the types of sugar before and after. ( 2 pts.)

What happened to sugar 2 when HCl was added ? Again, refer to
the structure of the sugar before and after. ( 2 pts.)

10.

11.

12.

13.

I4.

15.
16.
17.

9S

Carbohydrate Test - Key

0WD

03’?!

B
D

Yes, there was a blue color at first that became lighter as the
helical structure of the starch reacted with the iodine over
time.

Amylose - which is helical in structure.
Amylopectin - which has a branched structure.

Glucose has a positive test and turns red because it is a
monosaccharide.

Sucrose yields a negative test and remains blue because it is a
disaccharide (Oligosaccharide) which does not react with the
Benedict’s solution.

The control was distilled water.

The reaction with Benedict’s is negative - remains blue.

The iodine reaction is also negative - remains yellow.

The control is a check to make sure the reagents have not changed
the solutions. This is called a negative control if a positve
result is obtained something is wrong with the solutions.

Lactose di-/oli- milk energy/storage
Galactose mono- pectins energy

Sucrose di-/oli- sugar energy/ storage
Starch poly- potatoes storage
Fructose mono- fruits/honey energy

Cx(H20)y

C12H220113 C‘H120‘

Cellulose; Polysaccharlde

96

Carbohydrate Key - cont.

CHART
Sugar Results Results Type
A + - mono-
B - - oli-
C - + poly-
D + + oli-/poly-
E - + poly-
F + - mono-
18. A B D B F; These three sugars have a positive Benedict’s test
and a negative iodine test.
19. C B E: These two sugars are positive for the iodine test and

negative for the Benedict’s test.

20. Sugar B
21. Sugar B is only an oligosaccharide without a free aldehyde or
keytone group.
Sugar D is an oligosaccharide or polysaccharide with a free
aldehyde or keytone group.
CHART
Sugar Results Results Type
X - + poly-
X + saliva + - mono-
Y - - oli—/poly-
Y + BC] + — mono-
Z - + poly-
Z + H0] - + poly-
W + - mono
V + - mono-
W + V - + poly-
22. They have formed a polysaccharide.
Dehydration synthesis.
Both sugars are monosaccharides (reducing sugars).
23. Sugar X has undergone hydrolysis.
X was a polysaccharide before the saliva was added; now X has
been converted to monosaccharides.
24. Sugar Y has been hydrolyzed.
Y has changed from an oli-lpolysaccharide to monosaccharides.
25. Hydrolysis may or may not have occurred, probably not.

The sugar is still a polysaccharide; therefore if hydrolysis did
occur, it was not complete.

LIPIDS TEST

CHEMISTRY II NAME

 

SHORT ANSWER and COMPLETION

For questions #1 thru #4, identify which lipid group (class) is drawn.

 

 

 

 

1 pt. each

1.

2.

3.

4.

5. Which elements are lipids composed of? Why are lipids called

organic molecules? 4 pts.

Compare and contrast lipids and carbohydrates. Refer to how many
calories per gram, the differing ratio of elements, and list at
least three functions of each. 4 pts.

For the two structural formulas drawn below, identify each

‘ diagram with the specific lipid name. In which lipid class are

these two lipids found? 4 pts.

97

10.

11.

12.

13.

14.

15.

98

Explain what happens chemically during the hydrogenation of an
oil. 1 pt.

Compare and contrast fats and oils. State lipid class, physical
state at room temperature, and type of bonds between carbon
atoms. 3 pts.

List the five general functions of lipids. 5 pts.

At your age, what percentage of your daily caloric intake should
be in the form of lipids? As you get older should your lipid
intake increase or decrease? Why? 3 pts.

Compare and contrast neutral lipids and phosphollpids. Discuss
the chemical make-up of each, two functions of each, and give an
example of each. 4 pts.

What type of lipid makes up the plasma membrane and causes the
plasma membrane to remain flexible? 2 pts.

Draw the plasma membrane and explain how and why the membrane is
arranged in this way. 3 pts.

State the major function of the plasma membrane. 1 pt.

16.

17.

18.

19.

20.

21.

22.

23.

24.

25.

99

Name the other lipid found in the membrane that gives the
membrane some rigidness. 1 pt.

Compare and contrast waxes and steroids. Include structure,
functions, and give three specific examples of each. 5 pts.

What causes arteriosclerosis? Explain this disease. 2 pts.
What are steroids, vitamin D, estrogen, and bile salts derived
from? What is the primary metabolic precursor? 1 pt.

What is the purpose of vitamin D in your body? What kind of
lipid is vitamin D? 2 pts.

Compare and contrast testosterone and estrogen. Identify the
type of lipid, describe the general structure, and state each
one’s function in the body. 3 pts.

What do bile salts do in the small intestine? 1 pt.

State the name of the enzyme used in the lab to‘break down fats.
1 pt.

What did the enzyme break the fats into? Name the pieces.
2 pts.

Discuss how we tested the laboratory solution to determine if the
fats had been broken down. 1 pt.

100

26. Compare the results in the following situation. Test tube X has
bile salts and fat; tube Y has bile salts, fat, and the enzyme to

break down fats. What would you expect the results to be? Why?
4 pts.

YOU RUN A FAT DIGESTION EXPERIMENT AND HERE ARE YOUR RESULTS:

Tube Bile acid Lipid enzyme Fat pH before pH after

A yes no yes 7 7
B yes yes yes 7 '5
C yes yes yes 7 7
D no yes yes 7 6
E no yes yes 7 7

Answer the following according to the above results.

27. Which tube had the most fat digestion? 1 pt.

28. Which tube should have had fat digestion but did not? 1 pt.

29. Why does tube D show a change in the pH? Expain what has
happened. 1 pt.

101

Lipid Test - Answer Key

1. Phospholipid

2. Wax

3. Neutral lipid

4. Steroid

5. C, H, and 0. Lipids are called organic molecules because they

contain carbon and compose living tissue or are produced by
living organisms.

6. Lipids Carbohydrates
9 cal/gram 4 cal/gram
H:O Is > 2:1 H:O IS = 2:1
Energy store Energy source
Protection Energy store
Insulation Structural material
Cell membranes Carbon source
Biological regulators Plant cell walls

7. Testosterone; Cholesterol. Both are steroids.

8. The addition of hydrogen breaks the double bonds between the
carbon atoms making the oil saturated. This process turns the
oil into a fat.

9. Fats Oils
neutral lipid neutral lipid
solid liquid
saturated unsaturated

10. Energy storage, insulation, protection, structural, regulators

11. 30% ; decrease; Lipids have a high calorie and cholesterol
content which leads to circulatory problems in later years.

12. Neutral lipids Phospholiplds
glycerol + 3 fatty acids same + a phosphate group
energy store, insulation, support cell membranes, non-stick sprays
body fat, vegetable or seed oil lecithin ( PAM )

13. Phospholipid

102

Lipid Key - cont.

14. The plasma membrane is a lipid bilayer which contains protein
molecules. The hydrophobic tail ends are non-polar so they ‘repel’
water and align toward the center of the membrane. The hydrophilic
head ends are polar so they align on the outside where the fluids
(water) are. This arrangement allows for the regulation of water into
and out of the cell.

15. Forms a protective layer of cellular regulation.

16. Lipopolysaccharide

17. Waxes Steroids
long chain fatty acids 3 cyclohexane rings B one
B alcohol cyclopentane ring
protection, waterproofing biological regulators
beeswax, whale oil testosterone, vit D, bile acids

18. Arteriolsclerosis is caused by an abundance of cholesterol in the
arteries. This clogs the arteries and forces the heart to work
harder.

19. Cholesterol or 3 cyclohexane rings and 1 cyclopentane ring

20. Vit. D is essential for strong bone development. A steroid.

21. Testosterone ' Estrogen

steroid steroid

3 cyclohex. rings and 1 cyclopent. ring (same)
develop male sex. charact. female sex. characteristics

22. Break down fats into smaller droplets called globules.
23. Lipase was the enzyme contained in pancreatin.
24. Fats were broken into fatty acids and glycerol.
25. Determine the pH: if it’s acidic then the fat was broken down.
26. Tube X - no digestion, Just smaller globules.
Tube Y - would expect complete digestion as the enzyme would be

able to affect all globules.

27. Tube B

103

LIPID KEY -cont.
28. Tube C
29. Enzyme was able to slightly digest the fat. The digestion is not

as complete as in tube B due to the absence of bile causing less
surface area.

PROTEINS AND ENZYMES TEST

CHEMISTRY I I Name

 

CHOOSE THE BEST ANSWER FOR THE FOLLOWING MULTIPLE CHOICE QUESTIONS.
MARK YOUR ANSWERS ON THE SCANTRON SHEET.

1. What are the basic building blocks for all proteins?
a polypeptides

b. alpha amino acids

c beta amino acids

d simple sugars

2. What is the approximate molecular weight for protein
molecules?

a. 100 - 100
1000 - 10.000
6,000 - many million
many million - billions

 

b.

c.

d.

3. What kind of bonds link amino acids together?
a. carboxyl
b. glycosidic
c. amino

d. peptide

e. hydrogen

4. Which solution, that we used in lab, combines with,the free
amino group of amino acids and turns a purple color?

a. Ninhydrin

b. Xanthroprotelc

c. Pancreatin

d. Bradford’s

5. Which of the following is made up of two amino acids and has

one peptide bond?

a. tripeptide

b. protein

c. dipeptide

d. polypeptide

____ 6. Which of the following is composed of fifty or more amino

acids?

a. tripeptide

b. protein

c. dipeptide
d. polypeptide

104

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105

The class of proteins that yields only amino acids when
hydrolyzed is:

complex

conJugated

simple

polypeptide

Which of the following protein substances listed below is a
very harmful protein to our bodies?

viruses

fibrinogen

antibodies

arginine

phenylalinine

Which proteins listed below are very important structures
within our immune system?

viruses

fibrinogen

antibodies

arginine

phenylalinine

. What is the type of reaction that occurs between amino acids

leading to peptides and eventually proteins?
hydrolysis

denaturation

renaturation

dehydration

The prosthetic group on the amino acid is commonly the:
amino part

carboxyl part

R group

first carbon

. This test is used for determining aromatic amino acids. The

test uses nitric acid and yields a characteristic yellow
color.

Biuret’s

Xanthroprotelc

Ninhydrin

Bradford’s

. What is the minimum amount of protein that should be ingested

(eaten) every day?
39

12 g

50 g

20 g

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106

. This protein structure is formed when several globular

proteins are Joined together.
primary

secondary

tertiary

quaternary

. This structure of a protein is Just the amino acid sequence

chain.
primary
secondary
tertiary
quaternary

. This particular protein structure is the globular form of a

single protein.
primary
secondary
tertiary
quaternary

. This is the term given to a protein that has lost its

biological activity.
renaturation
denaturation
hydrolysis
dehydration

. We can best obtain all twenty essential amino acids from

eating a variety of:
bacteria

fish

meat

plants

each other (cannibalism)

. Which of the following would not be an example of a

prosthetic group?
nucleic acid
mercury 11 chloride
iron III hydroxide
sugars
phosphollpids

. When we cannot produce an amino acid within our own bodies,

this type of amino acid is called:
useless

nonessential

essential

-antigen

21.

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107

This type of protein yields amino acids and organic or
inorganic components when hydrolyzed.

simple

conJugated

cofactor

coenzyme

This is the chemical process used to break down proteins into
amino acids:

catalyst

dehydration

hydrolysis

denaturation

Amino acid biosynthesis can occur in:
animals

bacteria

plants

all of these

only a and c

. This test can be used to detect the presence of proteins. An

alkaline solution of copper II sulfate reacts with proteins
and yields a purple color.

Xanthoprotic

Biuret’s

Ninhydrin

Bradford’s

all of the above

This type of substance speeds up reactions without being used
up in - or consumed by - the reaction.

catalyst

carbohydrate

amino group

prosthetic group

. If enzymes were not present in our bodies, then:

reactions would occur at faster rates

reactions in the body would never occur

carbohydrates would be the only substances broken down
reactions would occur but at very slow rates

This protein yields amino acids and a prosthetic group when
broken down.

conJugated

simple

complex

quaternary

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108

. If an enzyme has a prosthetic group that is a complex organic

molecule, this group is called:
a cofactor

the active site

an amino group

a coenzyme

What part of an enzyme does a substrate bind to?
the cofactor

the active site

the coenzyme

the amino group

. Most enzymes are capable of binding to how many substrates?

one
two
three
many

. This enzyme acts in the small intestine to digest

polypeptides into amino acids.
trypsin

pepsin

peptidase

lipase

This enzyme digests fats and oils into fatty acids and
glycerol.

trypsin

pepsin

peptidase

lipase

. The enzyme that digests proteins in the stomach into

polypeptides.
trypsin
pepsin
peptidase

.lipase

This is the enzyme found in pancreatin that we used in the
protein digestion lab. The enzyme acts on proteins in the
small intestine that have made it through the stomach.
trypsin

pepsin

peptidase

lipase

109

35. Enzymes are responsible for:
digesting food

synthesizing proteins
speeding up reactions

all of the above

a and c only

00,059

6. The enzyme and substrate reaction works like:
a chain of beads

two cubes coming together

a lock and key

‘congress’ - functionally decrepit

QGU’QQ

FOR THE FOLLOWING SECTION MATCH THE CORRECT AMINO ACID TO ITS
ABBREVIATION.

.____ 37. glycine a Asn
b Phe

____ 38. methionine c. Try
d. Asg

____ 39. tryptophan e Iie
ab Gin

____ 40. phenylalinine ac. 180
ad. Gly

_____ 41. isoleucine ae. Met
bc. Phl

____ 42. asparagine bd. Trp

THE FOLLOWING SECTION IS A SHORT ANSWER SECTION. YOU MAY WRITE IN
THIS TEST.

43. List four ways to denature a protein. 4 pts.

44. Explain what is happening to a protein when it is denatured.

Include a definition and discuss what happens to the structure
and bonds. 2 pts.

45. Draw and label the basic building block of amino acids. Label
all four parts. 5 pts.

46.

47.

48.

49.

50.

110

Compare and contrast dehydration synthesis, hydrolysis, and
denaturation as they relate to proteins. Keep in mind the
mechanism ( what’s occurring ). 6 pts.

List four factors that affect an enzyme’s ability to function.
4 pts.

At what temperature will an enzyme begin to denature?
At what temperature will an enzyme be totally denatured?
2 pts

What is the two step process used by an enzyme during protein

synthesis? If you wish, you may draw and label this process.
2 pts.

According to the information in the lab on protein digestion,
proteases such as pepsin function best in low pH (acidic)
environments. Considering the stomach secretes a strong acid and
the duodenum receives a strong base from the pancreas, how does
this acid-base situation affect the pepsin’s activity in these
two parts of the body? 2 pts.

111

FOR THE FOLLOWING SECTION. ANSWER THE QUESTIONS BY REFERRING TO THE
GRAPH AND THE CHROMATOGRAPHY PAPER. ( Draw a line to connect the
plotted points. )

51.
[AI

52.

53.

A 1.0 —I
b 0.9 -l
s 0.8 -l
o 0.7 -l
r 0.6 —l
b 0.5 -l
e 0.4 —l
n 0.3 -I
c 0.2 -l
y 0.1 -l
0.0 I ------------------------------

Concentration (mg/ mL)

Using the graph above, what is the concentration of protein A
if the absorbency is 0.7 ? 1 pt.

What would be the absorbency of protein B if the concentration is
0.25 mg/mL ? 1 pt.

What is the name given to this type of graph drawn above? 1 pt.

112

SAMPLE CHROMATOGRAPHY PAPER

 

solvent front

—--------—--~----------------------------—--—-—---------------“--

I

9 purple I 0 purple 9 purple

I I 20mm I I

I 16mm I I 16mm I 16mm

I I 0 purple I 0 purple

l I I l l

I I I 10 mm I I

I I I I I

I l l I l

I I I I I

I I I I I

I * yellowI I I a yellow I * yel.

I I I I I I I I

I I 2mm I I I I I I
Amino I I I I I I unknown I Iunkn.
.Acid IA [B I IC I I 4 1 I i # 2

 

Using the sample chromatography paper above, determine the Rf
factor for each known amino acid. 3 pts.

A B C

Which amino acids (A,B,C) have free amino groups? How do you
know? 2 pts.

Which amino acids are found in unknown # 1 and in unknown #2 ?
2pts.

10.
11.
12.
13.
14.
15.
16.
17.

18.

37.
38.
39.
40.
41.

42.

)'

)DDWODO)OWO

O

AD
AE
BD

Protein and Enzymes Test - Key

19.
20.
21.
22.
23.
24.
25.
26.
27.
28.
29.
30.
31.
32.
33.
34.
35.

36.

11

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)

A

O

114

Protein and Enzyme Key - cont.

43. Any four of the following: temperature, pH, lead salts, mercury
salts, alcohol, and acetone.

44. Denaturation is the loss of a protein’s biological activity. The
proteins lose their structure (from 4° to 1°) which causes this loss.
However, the peptide bonds are not broken.

45. ' Alpha carbon
Prosthetic group Carboxyl group

Amino group

46. Dehydration synthesis - amino acids bond to form peptide bonds
which yield proteins plus water.
Hydrolysis - proteins plus water yield amino acids by breaking
the peptide bonds. '
Denaturation destroys the structure of proteins, thus losing
activity, yet the proteins are not broken down.

47. [enzyme], [substrate], pH, and temperature.
48. 45°C; 55°C

49. 1) The enzyme plus two amino acids (substrates) Join at the
active site on the enzyme.
2) The enzyme catalyzes the reaction forming a peptide bond and
releases the bound substrates as one new protein.

50. The pepsin is very active in the stomach breaking down proteins.
However, when the pepsin-protein mixture enters the alkaline
conditions of the duodenum, the pepsin loses its ability to catalyze.

51. .5

52. .3

53. A standard curve
54. Amino acid A 16/20

Amino acid B 2/20
Amino acid C 10/20

II II II
DOC
GHQ)

55. A and C; This is indicated by the purple color.

56. Unknown #1 has amino acids A B B
Unknown #2 has amino acids A, B, B C

NUCLEIC ACIDS TEST

CHEMISTRY II NAME

 

CHOOSE THE BEST ANSWER FOR THE FOLLOWING MULTIPLE CHOICE QUESTIONS.
PLACE YOUR ANSWERS ON THE SCANTRON SHEET.

1.

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A section of a nucleic acid is composed of a nitrogenous base
and a five carbon sugar. This section is called a:
nucleotide

nucleoside

polynucleotide

polynucleoside

This type of nucleic acid is found as a double stranded
helix.

tRNA

rRNA

DNA

mRNA

mDNA

This type of nucleic acid looks like a cloverleaf, has an
anticodon end, and an attachment site for an amino acid.
tRNA

rRNA

DNA

mRNA

This type of nucleic acid combines with proteins and forms
the ribosomes that carry out translation.

tRNA

rRNA

DNA

mRNA

This type of nucleic acid has deoxyribose and thymine.
tRNA
rRNA
DNA
mRNA

This nitrogenous base is a pyrimidine found only in RNA.
adenine

cytosine

guanine

thymine

uracil

This nitrogenous base is a purine found in both DNA and RNA.
This purine is also a maJor component of the mononucleotides
responsible for storage and energy release within the cell.

115

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116

adenine
cytosine
guanine
thymine
uracil

This basic building block of a nucleic acid is composed of a
five carbon sugar, phosphoric acid, and a nitrogenous base.
nucleoside

polynucleotide

nucleotide

polynucleoside

Protein synthesis occurs in this part of the cell.
nucleolus

nucleus

mitochondria

cytoplasm

membrane

. This nitrogenous base is a pyrimidine found only in DNA.

cytosine
guanine
thymine
uracil

. This nitrogenous base Is found only in RNA.

cytosine
uracil
guanine
thymine

. This type of nucleic acid has codons.

tRNA
dRNA
rRNA
mRNA

. DNA has the ability to copy itself. This process is known

as:

translation
duplication
transcription
replication
dehydration synthesis

. When small pieces of the DNA code are copied into an RNA code

this process is called:

QOU’DI

QOU‘O’N

0.

11?

translation
transcription
dehydration synthesis
duplication
replication

. When mRNA is ‘read’ and used to make proteins this process is

referred to as :
translation
transcription
duplication
replication
redundancy

. RNA molecules have molecular weights that vary greatly in

size. The highest molecular weights are around:
250

2.500

25,000

250.000

. DNA molecules are some of the largest known having molecular

weights in the range.
one million
ten million
one billion
ten billion

. Which process requires the presence and use of mRNA, tRNA,

and rRNA?
replication
hydrolysis
transcription
duplication
translation

. What would be the complementary strand of DNA if one partial

strand has the sequence AACGTTCG?
UUGCAACG
TTCGUUCG
TTGCAAGC
CCTUGGTU

What is the anticodon sequence if the codon sequence is AUC?
UAG
TAG
UTA
TGA

118

SHORT ANSWER SECTION

21.

22.

23.

24.

25.

26.

Explain what semiconservative replication is. You may use a
drawing to help explain if you wish. 2 pts.

Explain why the genetic code (codons) is said to be redundant.
1 pt.

State the maJor functon of DNA and the maJor function of RNA.
2 pts.

The sequence shown below is a SINGLE strand of DNA. Below it
write the second (daughter) strand. 2 pts.

A T G T A C C A A A C A T T A A T C A T A C T A A A A

How many codons are present is the above strand ? 1 pt.

For the sequence that 1 have drawn in #4, write below the mRNA
sequence. On your mRNA sequence, circle where the start and stop
codons are. 3 pts.

Using your sequence in #5 and the given table, show what each
anticodon would be for each mRNA codon. Now draw the amino acid
sequence for the protein. ( Hint: remember about the stop and
start codons.) 5 pts.

10.

21.

22.

23.

24.
25.

26.

119

Nucleic Acids Test - Key

B 11. B
C 12. D
A 13. D
B 14. B
C 15. A
E 16. D
A 17. C
C 18. E
D 19. C
C 20. A

Parent DNA ‘unzips’ itself and picks up amino acids to form two
new daughter strands. The parent DNA makes up half of the new
strands thus it is conserved.

The codons are in triplets and have 64 possible combinations of
three. But there are only 20 amino acids - so virtually all
amino acids have more than one anticodon sequence.

DNA has the genetic code and passes on this information.
RNA is responsible for making proteins .

TAC ATG GTT TGT AAT TAG TAT GAT TTT 3 Nine

UAC AUG GUU UGU AAU UAG UAU GAU 000
Start is AUG; Stop is UAG

AUG UAC CAA ACA UUA AUC AUC AUA CUA AAA
met-val-cys-asn
( protein )

APPENDIX G

APPENDIX G

LOOKING AT THE SACCHARIDES IN OUR FOODS

Describe this food product.

What is the size of a typical serving?
How many grams of carbohydrates are in a serving?

Look carefully at the ingredients. List each type of carbohydrate
in this food product. For each carbohydrate state its particular
function -- energy, carbon, storage, or structural. Then identify
the type of saccharide -- monosaccharide, oligosaccharide, or
polysaccharide.

CARBOHYDRATE FUNCTION TYPE

Which sugars in the above list would you think are reducing
sugars? Explain your reasoning.

Which sugars in the above list (#4) would give positive results in
the iodine test? Explain your reasoning.

Knowing that the best carbohydrates to ingest are the structural

and energy ones, which of the above carbohydrates are good for
you?

When would a storage type saccharide be good for you?

120

Oral Report on Steroids

Complete a literary survey to find an athlete who has used or

abused steroids and report the following.

Identity of user

The type of steroid used

The purpose for taking the steroid
The potential side effects

Other pertinent information

Author and/or references

Possible sources include:
Newspapers
Sports magazines
Health/Nutrition magazines

Exercise magazines

121

Nucleic Acids - Key Terms

Develop questions and/or problems for each of the following:
DNA B RNA
Comparison
Components
Structure
Nucleoside
Nucleotide
Pyrimidines
Purines
AMP,ADP, and ATP
mRNA, tRNA, and rRNA
Replication
Transcription
Translation
Protein synthesis
Codon
Initiator
Terminator
Cellular structure
Protein structure
DNA sequencing
Daughter strands (cells)
Hydrogen bonds
Molecular weights of DNA and RNA

Base pairings of DNA and RNA

122

APPENDIX H

APPENDIX H

The only difference between these two reactions is in Ihe kiml of linkage Chapter 10
by which glucose units are joined in :nnylnse and in t‘vllulnm'. ln :nnylnree, llle Carbohydrate:
linkage is by an a -i,4- bond; in cellulose, the linkage is by a U-l,-l- bond.

This may not seem like a very big difference. After all, most of the
atoms in both molecules are in exactly the same relationship to each other.
In fact, there is a very great difference. If you think about the role of starch
and cellulose in your everyday life, you'll begin to realize that. llumans can
eat starch and digest it easily. Bread, cereal grains, flour, and many other
parts of our diet contain starch. We require these foods as sources of carho-
hydrates in our diets. llut cellulose-containinu mater ials“ leaves, mass, and
cotton, for example-are not parts of our diet. if we should happen to eat
any of these materials, they pass through and out of the body unchanged.
What this means is that the human body has no way of digesting cellulose,
although it can easily break apart
its-cousin, starch. How can we
eXplain this difference?

Our bodies contain just the

GHQ?)
right enzymes. The enzymes in drooQQQQCLYKIW b)?
I

this case are compounds that will

attack the o-1,4~ linkage and I .98

break it apart. The reaction is g;\5;‘¢3chze 83“

shown here. It is the first step U r' (3%

- - - W I J} ' W55]

in digestion that occurs when- I}
a a” ,
“a! 0%,21151190

ever we eat a food containing
starch.

You’ll notice that the en-
zyme chops off two glucose _ A A
units at a time. in other words, (a)
maltose is one of the first prod-
ucts of the digestion of starch.

But the enzymes that can
break apart an a-l,4- linkage Cb Q3
cannot do anything wrth a mQDCD (be T

8
B-l,4-linkaue. Canyon (DU) (O‘DL (DL 8 8
"to i) ‘8) 8 8
8
8

Hydrolysis
(catalyzed by B -amylase)

think of any reason that Q) 02)
this might be so? (A par- Q) “A. Q) ,
tial answer will be found (p 0000 a. I]
on page 203.) The enzymes (5)0000“)an 1&3ou e (9 (5)
that take starch apart for (5) (9 W l11'le) (9
us, then, are no help in (5) & “flied? (9&6)
trying to digest cellulose. C9 (5)

These animals other (5)
than humans that can di-
gest cellulose do so for one 8 30.3%
of two reasons. First, they 8 (X) (I) (I)
may have the right enzymes by
themselves. This means 1")
having enzymes that work I-‘iumc I06 lligeslion of Starch

123

1124

lllIILISI ltlll Ul‘ L/llllllilli'llll/llLS

N'lYLUSE

X llzt)

 

 

I
Il/llltlSlZ IIAIIIIIIIIIISIZ llllAllCllED 0R fl-DEXlRlNS
ULU‘ULU IILu-IILII-IILU GI|_U I 6
<—-——— a- -
O-l’H-BOIID/ GLu-GLu-GLU
lezl)
ULIICUNIYLASE JeumN/ISE.
lle +
LU. oar-LL61. AND
HALIASE
til ,I It‘LIfiIZ
lllll l3 4
LACI'ASIE /'7 Sucrmse
//
fllw
I
LACIOSE UALACIUSE FRUCIOSE Sucnose

More:

AllI'LIII‘LCl ill

 

GLYCUGEH

  
  
  

SAlemzv (I-DIIIII) N-IU PNICREATIC
u—N-Irmse‘ (iIIIESleAL LUI-IEII)-

SI’IZCIFIC FOR u-l.'I-GLUCOSIDIC

nouns. lurenreurares ARE CALLED
liexmms-

 

 
 
 
    

ALL ENZYMES UI'IDEIILIIIEU ARE ill llltE liltUSll‘liUllDlElt CELLS OF ME lNIESTlNAL WALL

125

W~

Ll lD llDC.)

Dari ni'l'l‘on '.
W

Ollxcr lam) 'lo LiflcltrleJ‘tl.’
W

ll ll dro [)ho lOI‘C
ll LI 4 (‘o{)l‘\i l I'C'

Po lav

\\l0(\~ Polar

PW II-Tallcl uaci Is (In CKlI'P‘ml‘K

otct d 0? 'l'lng gamer (,_\ s'i‘ruc-l-u Ire I? __ C,,<)
‘ 0M
(film we, R {5 generally 0t htldl‘o carbo n con'lotfninj

onxlwhcv-c *Ct‘orn~ l-l-o 9.x amigo“ Ct‘loms, 11,1
shook C/l'Ytin '80.“? Ltcid’) are. sometimes Call ed
‘l’lM. VOla-l-u'lr; Quilt, OciclS (VFhl- Nearlt’ all
'lrol‘ltl O‘CI'GLS lMUC (In LLVCn nunaber- 0i: CQ‘lOmg

126

26 Chapter 2 / I'hysical I’ruperties .rnd lunrtional Rules of lipids in Membranes

rrrerrrbrarre proteins are often inserted into and through the lipid
matrix have further contributed to our present understanding of
membranes, resultiru; in Ilre Singer and Nicolson (1972) fluid mosaic
model, a refined version of which is shown in Figure 2.1.

The ability of lipids to assume the basic bilayer organization is
dictated by a unityinp characteristic of membrane lipids—namely,
their mrrplrrprrllrrc character, which is indicated by the presence of a

Plasma rrrrrrrrtrrarrc

 

 

 

 

Cylusol

Figure 2.1. 1 he topography of membrane protein, lipid, and carbohydrate in the fluid
mosaic model of a typical encaryotic plasma membrane. l‘hospholipid asymmetry
results in the preferential location of plrosphatidylrtlranolamine and phospha-
tidylserine in the cytosolic monolayer. Carbohydrate moieties on lipids and proteins
face the extracellular space. Ar]: represents the transmembrane potential, negative

inside the cell.

127

472 BIOLOGICAL DYNAMICS

  
 

 

e ' o \
' Basrc groups of phosplrolrds, \
as choline, etlranolamine \

' Phosphate groups of phospholipids \\ It?

aEnd of fatty acid side chains of

phospholipids

1 Cholesterol

 

  

 

 

 

 

 

 

, q ,rf-r rrrv rim: r" ------------------------------ '-
I 7;". ' l t I
I, '\l'.I¢fl :3 li' .llll: WMVW
I if I l ltlli.’ '. Proteins
/ l‘ll' "Eli‘s-- I’ fl. W
/ " r' r r: z.‘ 25 A (20 A)
I r, ‘
I] "r’oc‘elwl t’ i W
,’ r-rriI.-Il.l;’”T-I.l.‘r .. -
I 'u‘: Ira-"J a," .‘. 1' I
, 1...... ..
/ . - a ____________ --- -- --- __
/ . u-{T‘ r v
I r, ~' I.”
II I (gill i
I I. . ... >~ c.“ 'y
/ 7s A unit 1;“ 1...:x-g‘s‘rlg , I, r ‘ Lipids
\ membrane {all " a if 25 A v v v *v‘, ‘,‘ US A)
\\ I" _ l . (. 313$" Ii
\ .‘,‘.‘.l.:r‘,l\'rlf' r43
\ .r t‘ J
\ rear --‘ll.’. ______________ II... ..- L --- ..
\ rl \' {3.113;} ‘I l l __
5;; “001150” it WW
\ |' .
\ h; I starrrrnr-r 1 23', A l’ .
1 tfllclttS
\ rt." Wilton ’ W (20 N
a '5‘6 " 'i
\ r registered-r ~ M
\\ 51122:”? or 1.2. M l
\.,';".I_'r 'i.‘ _________________________________

Fig. 17-26. Chemical diagram of unit membrane and membrane as seen In electron
microscope. (After Uavsorr, Darrielli, Robertson; micrograph courtesy of W. Stoeckenius,
Rockefeller University.)

of the cell (Fig. l7-27l. this is what one would expect if the rrriddle layer of the sand-
wich is rrrade of a birrrolecolar leaflet of lipid because such a layer would beheld
together only by the relatively weak van dcr Waals forces between the nonpolar lipid
side chains.

in recent years, however, workers in the field of rrrerrrbrarre structure began to have
sorrre second thoughts regarding the biological relevance of the Davson and Danielli
rrrodel and the general applicability of the unit membrane theory. “this has led to a
variety of different, though as yet imprecise, models of rrrenrbrane structure (Fig. l7-Ziil.
Let us summarize the evidence in favor of a more corrrplex Iormulation of membrane
structure.

1. The chemistry of membranes varies considerably. It rrrust be obvious by now
that membranes can be, and have been, isolated. We can strip off the plasma nrenrbrarre
of mammalian cells and we can get the outer rrrerrrbrarre of the bacteria in the form of
Spheroplasts. We can isolate endoplasmic reticulum rnerrrbranes in the iorrn of micro-
somes, as detailed in Chapter l5; nuclei can be isolated and their membranes obtained.
Mitochondria and chloroplasts have been isolated: in the case of the former the outer,
limiting membrane of the mitochondria has been separated Irorn the Inner, cristae
membranes with their knobs (see Chapter 13); whereas in the case of the latter the
chlorophyll-containing laruellae have been obtained. Only a few membrane systems
have been studied so far hour the point of view of their protein-lipid content, but the

1128

Metabolic and l'recorsm I'unctions ol the Sterol Molecule 3
. . -.,l
l: l" l' 'l' R Antherrdiol
EN O"
Fl Q1 °
”0 I \/ \ \ §
Bite Acids / HO 0

 

- HO
OH CH20803 r—> Cordenotrdes pOH
. $050” ((0 l/ /
2
CH C
HO" II “0” C27 0
a - Ecdysone
a-Cyprinol O
(Coeloconthl I
- . CZI
l 7 O D Vitomrns
II
on con 0’
I Progesterone
, . r
HO’ ‘0” c=0 0
HO 'OH r
Cholrc Acid
0 f E :l: 7
i ll 0 C2‘ of Cl9
Nil -
I Cortisol Androstenediono

(Cllzlz 503“

CH
Tourocholrc ACId &
Fr' e 1.1. Fun ‘li rnal
gm 1. r HO cm

evolution of the sterol

molecule. Estrodiol

side Chain. Thus the omnivorous cockroach dealkylates ergosterol or
C29 plant slerols to 22-dehydrocholeslerol, while Derrrresles vrrlpr'rrrrs,
an obligate carnivore, lacks—because it does not need—the requisite
dealkylating enzymes (Clark and liloeh I959).

An extensive examination of marine inver'teln'ates (sponges, gorgo-
nians) has uncovered a bewildering variety of side-chain-modilied
sterols. Structures hearing additional alkyl or evelopropane groups at
six of the eight isoor'tvl sterol side-chain positions have been ideo-
tilied (l)jerassi et al. WW). It has been suggested, and to some extent
documented, that the pliospliolipirls of such marine or'rganisrrts

129

30 I CHAPTER 5

Table 5-5. Modrlrt‘d tIOtt-n lrrrrrjirorinl rpmrps ol [)Htlt‘ttt".

 

Group Modttled

 

 

 

 

 

 

 

40.“- NOII- u N‘ -.- _. . _ --
POJHJ N-Mctlryl N- Ulrrretlryi II iririiettryi

Arg Arg
His
Lys Lys Lys

Ser

Tirr

Tyr

 

 

 

 

'Modihed and reproduced, with permission. Irorn Uy R, Wold F:
Posttrarrstatronal c0va|eot modification of proterus SCrence
1977;190:890 Copyright Q 1977 by the American Association
for the Advancement of Science.

yond the scape of this chapter, their presence can corn-
plicatc the dclcrrrrination oi prirrrary structure.

Primary Structures of
insulin & Ribonuclease

lrrsuiirr consists of 2 polypeptide chains linked co.
valcrrtiy by disultidc bonds (Hg 5 -‘)). ’l be A chain has
an N-tcrminal Lily and a C-tcrrninal Asn; tlrc ll chain
has Phe and Ala as the N- and C-tcrminal residues, rc-
srrcctivcly. When insulin is oxidized with perfurmic
acid. the disultide bonds linking the A and It chains are
rurrturcd. iioth chains are biosynthesizcd as a single
polypeptide chain, proirrsulin, which after formation
undergoes proteolytic processing. forming insulin.
(see Chapter 5|).

Ribonucleasc consists of a single chain of l2-l
residues witir Lys as the N terminus and Val as the C
tcrrrrirrus. Eight cysteine residues are joined by
disultidc bonds. forming 4 cross—linkages in the
protein (Fig 5- l0).

DETERMINATION OF SECONDARY 8r
TERTIARY STRUCTURE BY X-RAY
CRYSTALLOGRAPHY

While various techniques (cg, Optical rotatory dis-
pcrsion. tritiurrr exchange of labile protons) forrrrerly
were much used to inter the presence of lrclicai struc-
tures in proteins, these have been largely supplanted
by the powerful technique of x-ray crystallography.

 

S- S—
l I —2°l
-- —2r
0 til
5

l!)

A chain { glycine

~30

 

i
S
8 chain { phenylalanine l.___———

7

Figure 5-9. Relationship oi the A and U chains ol human
insulin.

e g . a g a n »_ II n .0 n u D C I

 

AM are |,._ rworrra1rrrr-rr-nor A0, 3' --1nc-$rrva- Mo. \
O_ ..-- __.._____._ ‘ar n
(a V _: W I
.... -__...__.___._J' M ”

  

 

Ir
0
”D
r
r
O
t'

rr
. ' u}; r'c.;;r—: dis-fiv- '7" for- -N m 5"
-.'-n F \

' 'V‘A
., ."r_:;"r. M3;
' ." ’ ._ "l " ...]
ICrS'uu ml. or -- ott- -r‘.r:~r o I.
- i r ,

N no —- - -—-- .-
' ,.

 

   

 

 

 

 

 

 

_-—
.....-

u “I“- Doe-Vao- Iro«hr-Asp-\Ml '0‘:.'.' ('e- li-‘Ao'lyl tw- b-IA:;-Ar"

 

Flgure 5—10. Structure of b0vine ribonuclease. Twoodi-
rrrrvosronni schematic rharparn showing the arrangement
ot the ills uttide hoods and the sequence of the amino acid
residues Arrows indicate the direction of the peptide
chain starting from the amino end (Reproduced. with per-
mission. irorn Srnyth DG. Stein WH. Moore S: The se-
quence oi arrrrno acid residues in bovine pancreatic ri-
trorrrrrtlr-arar lievisiorrs and confirmations. J Biol Chem
1963238227 )

 

X-rays are directed at a crystal of protein and generally
also at a derivative of that protein which contains an
added heavy metal ion. The rays are scattered in a pat-
tern that depends upon the electron densities irt differ-
ent parts of the protein. images, collected on a plroto-
graphic plate. are translated into electron density maps
which. when super irrrposcd one on another. pcrrrrit thc
crystallogtapth to construct a laitlrfui rrrodcl of the
protein in question. Although time-consuming. ex-
pensive. and requiring highly specialized training. x-
ray crystallography rcvcals detailed, prccisc Views of
the orientations of all the arrrirro acids in rrrarry
proteins. its corrtribrrtiorrs to our present-day concepts
of protein structure can hardly be overstated.

DETERMINATION OF OUATERNARY
STRUCTURE

Determining the quaternary structure of oligorncric
proteins encompasses determining the number and
kind of prorurncr‘s present. their mutual orientation.
and the interactions that trrritc them.

As long as oiipomcrs do not undergo denaturation
during the procedure rrscd to determine their molecu-
lar weight. rrrarry methods can yield molecular weight
data for oligomcrs. 'i'hcsc sarrrc techniques may be
used to determine protomcr molecular weight if the
oligomcr is lirst denatured.

Uttracentritugation

Developed by Svcdbcrg. this method measures
sedimentation rate in an ultracentrilugal iicld of
around ltI‘ x g. It has tended in recent ycarstobc rc-
piaccd by less complex techniques.

Sucrose Density Gradient
Centritugatlon

l’rrrlcirr standards and unknowns fttC layered over a
5- 2(‘ Jo sucrose gradient iii a plastic tube and ccn-

130

Vii-THU” gU/l-DNW; Baez/ms ox: NUCLEIC

/{‘LII)S NRC: MUCLE'OTIDE’S

 

H TYPICFIL. a/UC/ce’ofloe":

 

AL 7’ P
N/i'e
I ..-
/ \ / Bast
N, L 5C (ADE/VINE)
r, ”H
II C,\\ a / C. \
- ’ 0" ' ,
0§0g~0170~o - rim
0 l O 11
II t ‘. i ..
P/TLOSPHH7ETS C'T—fl C1, CRIBOSC)

130

.-"" / ’7 .;’1
lH-c: DWI-MAM; [)Locrrs or: NUCLEIC

l4¢lD$ NRC: NUCLEO’T'IDES

 

H TYPICFIA— “Mac; AEOT/DE.‘

my?
NHL 1
r
QSL:
{\i‘/L\C/’ \ B
i, ,ll \rcr-r (”DEN'NE)
,3 . a
- ”Cc N/C\/\I /
.. Q” ' ,
ogO‘K‘O-fio—O- Ell-r.
g (30 a I /O
x \\ r’
\fll/CQ' p r-‘l /C\l'l SUGIHR
PWSP/{H7ES C7—- C-u Gamma

131
230i.

Pm! II

Bio clremr‘s (I y
Figure Page

 

 

 

 

(h) I’leated sheet (U oarraugenrenl)

Figure I 2.3

Geometric ('rrnfigmalirrns of a I'roteiu Molecule

132

 

Eukaryotic Colts: the Nucleus 27

DNA v

rrbosmrat
RNA
(rRNA)

   
 

nucleus
”WA is

.ssetnbled
Into ribosomal
subunits In

ClepluSrtt

 

messenger
RNA
(rnthA)

Bro nucleus

......0
i a2.\\\

\\Hh,,,r‘~'1"' -—-—- '
\
pore
/ /
rrtrnsorrres triad
rnilllA IIIBSSJIUC and
nuclear aSSerrrbte proteins
envelope

Figure 4-14. the major events in cellular synthesis (see text),

DNA) and replication (duplicating the
DNA) and proteins that regulate or con-
trol those activities. Although many at the
enzymatic nonhistorru proteins active in
transcription and replication have been
successfully isolated and biochemically
characterized. little is known as yet about
the nonhislono proteins regulating nu-
clear lunctions.

Suspended within the chromatin ot
the nucleus are one or more irregularly
shaped bodies. the nucleoli (singular.
nucleolus; Figs. M and 4-13). the nu-
cleotar material is so densely packed that
Its boundaries are easily traced even
though no membranes separate the no
cleolus trom the surrounding ctrromatin.
two maior components. called simply the
mrcteolar fibers and nucleolar granules.
are visible inside the nucleolus. the nu-
cleotar tibers are indistinct and ditticult to
trace in electron micrograptrs; generally
they appear to be somewhat thinner than
cinematin tibers. the nucleolar gran-
ulos. In contrast. are distinctly visible
Inside the nucleolus as small spherical
particles about halt the size at cytoplas-
mic ribosomes. Frequently. spaces con.
taining chromatin tibors extend into the

nucleolus. giving parts of the structure a
more open. coarsely coiled appearance.
lth‘SlltfilltUHS into tttlcltntlm structure
and lurrrttrurr have cslalrlrtttrrrrt that the
Iitrrils and granules are the trrrrrphological
lorrns taken by successive steps in syn-
thesis ot the RNA at ribosorrres and the
assembly at ribosomal subunits, both at
which take place in the nucleolus the
overall size and shape at the nucleolus
and the distribution ol fibrils and granules
inside it change as cells go through their
cycles at growth and division

the nucleus lunctiorrs as the ultimate
corrtrot center tor cell activities (F ig. 444).
Within the chromatin, the intorrnation
required to synthesize cellular proteins
ls coded into the DNA. Two primary
kinds oI inlorrnalion are coded in the
DNA sequences. the directions tor matr-
lrrg proteins are spelled cut by a code
that uses the tour DNA nucleotides. three
at a time. to term the code words F. nelr
three-nucleotide code werd stands tor an
amino acid Reading the cmin words in
sequence along the DNA spells out the
sequence at amino nerds in a proterrt.
these protein'encnrlrrrg regions are
duplicated into ltNA cupres called mes-

mRNA

crow

note-t chain

In
'Q‘t /

t.“{
transfer
RNA: ttltNAs)

\K.
65 ® arias:

serrger RNAs (mRNAs), which carry the
directions tor making proteins to the
Cylrrptasrn.

Other UNA regions store the direc-
lions tor making two types ot accessory
ttNAs that act in parts ot ttre protein
synthesis mechanism. One. ribosomal
RNA (rRNA). terms a part oi the ribo-
somes. the RNA-protein structures that
assemble amino acids into proteins in the
Cytoplasm. the second. lransler RNA
(tllN/t). binds directly to amino acids
(luring protein synthesis and provides the
necessary link between the nucleic acid
code and the amino acid sequence of
proteins.

. Synthesis ot the mRNA. rRNA. and
"WA copies at DNA. called transcription.
occurs wittrin the cell nucleus. Following
transcription. the RNA copies pass
through the nuclear envelope and enter
the cytoplasm. Messenger RNA. once in
the Cytoplasrn. attaches to one or more
rihosonres the ribosomes then assem-
hte amino acids into proteins. using the
inlorrnatiort carried in the attached mRNA
as a guide. In this synthesis. called
trarrslarrnn. a titresonre starts alone and
or on rnttNA rrtoleculo and moves along

APPENDIX I

APPENDIX I

CHEMISTRY 11 PRE LAB: STUDY OF SACCHARIDES

PURPOSE:
To determine the chemical and physical properties of saccharides.
OBJECTIVES:

1. Using the Benedict’s test, determine whether certain
saccharides are reducing sugars or not.

2. Using the iodine test, determine if sugars are helically
coiled or branched polysaccharides.

3. Test known sugars in conjunction within unknown plant samples
to determine if the sample is a reducing sugar or a helical poly-
saccharide.

4. Assay to determine the effect of the enzyme amylase and acid
hydrolysis on saccharides.

BASIS FOR THE FIRST TWO CHEMICAL TESTS
Benedict’s Test

The Benedict’s reagent contains Cu“, a strong oxidizing agent.
Cu++ + e— ------------ > Cu+ reduction rxn
Basically the copper II is in an alkaline solution which promotes a
reaction with the linear forms of sugars which cause the copper II to
be reduced. When this occurs the Benedict’s solution turns from blue
to red and forms a precipitate. (see lab for complete discussion)

Iodine Test

Iodine is able to complex with helically coiled polysaccharide
chains (as opposed to linear chains) which converts the reddish-yellow
color of iodine to a bluish-black color. (see lab for details)

Assignment
After you have completed reading the lab, use your notes and the
tab to complete the following outline. Wherever you see a hyphen (—)

complete the statement or a colon (:) write in the definition. You
may use examples or write in any additional information you choose.

133

 

134

I. Saccharides are -
A. The general formula is -

B. The three main functions of saccharides are —
1.
2.
3.

11. There are three major groups of saccharides

A. Monosaccharides are -
. Main function is for -
. Two forms are —
. Most are white crystalline monomers that are soluble in H20
. Examples
a. glucose:
b. fructose:
c. galactose:

.waH

B. Oligosaccharides are-
1. Function is mainly for -
2. Most are disaccharides
3. Have glycosidic bonds which are -
4. Examples
a. sucrose:
b. maltose:
c. lactose:

C. Polysaccharldes are —
1. Main function is -
2. Have glycosidic bonds
3. Can have three forms -
a.
b.
c.
4. Hydrolysis of polysaccharides may yield -
5. Examples
. starch:
. dextrin:
glycogen:
cellulose:
chitin:
inulin:
. pectin:

QNGQOO’O!

DIGESTION OF FAT

PURPOSE

To demonstrate the relationship of the pancreatic enzyme lipase
and the steroid bile.

OBJECTIVES

To explain how lipase and bile work together in the breakdown of
fats.

To determine the end products of fat digestion.

PROCEDURE

1.

Identify three test tubes as 1, 2, and 3. Put 10 mL of distilled
water in each of the test tubes, then add a few (3-4) drOps of
Olive oil.

2. To test tubes 1 and 2 add 2 mL of the 5% bile salt solution
(sodium taurocholate).

3. Add SmL of the 2% pancreatin solution to test tubes 1 and 3.

4. Check each of the solutions with Hydrion paper. Solutions should
be neutral. If not. adjust with a minimal (trace) amount of
sodium bicarbonate if acidic. (use more enzyme if basic)

5. Place the three tubes in a water bath (40°C) for 30 minutes.

6. Check the solutions for a change in pH with the Hydrion paper.

7. Once tubes are in water bath, repeat the same procedure using
coconut oil and place in water bath immediately and check the
time. Compare your findings.

RESULTS

1.

What changes occurred in tube 1?

 

 

135

136

2. In tube 2?

 

 

3. In tube 3?

 

 

4. Account for the differences: use your worksheets as a reference.

 

 

TEACHER’S GUIDE TO GEL PERMEATION CHROMATOGRAPHY

AUTHORS:
Written by:

Clarence H. Suelter Michigan State University

Tested and revised by:

Michael J. Brundage Lapeer East High School

Mary M. Fowler Clarkston High School

Van A. McWilllams Stockbridge High School

Marie E. Rediess Algonac High School

Tamara J. Voss East Lansing High School
W:

The student will be able to define and discuss gel permeation
chromatography.

Upon completion of this lab the student will be able to separate
small molecules from large molecules using gel media.

Students will be able to collect equal samples of solutions and
detect concentration variance of contents using a spectrophotometer.

W:

Igggngp_gngpgggtlgn: Sephadex takes a minimum of three hours to
swell. Sephadex may be made in advance because it stores well
providing it does not dry out. If the teacher prepares columns,
the lab can be completed in 50 minutes.

sggggn;_1§p_;1mg: If students prepare columns two lab periods
will be needed. With columns prepared beforehand, the separation
and spectrophotometric work can be easily completed in one lab

period (50 minutes). Stopping between parts I and II is ideal
for a two day lab.

W:

1. To prepare each 100 mL Tris buffer of pH 8.0, place 0.117 g of
Tris base in 50 mL distilled water and 0.236 g of Tris HCL in 50
mL distilled water and combine to make 100 mL of buffer (Check
pH). You will need to make

137

138

100 mL buffer for rinsing each column. You will also need 100 mL
of buffer for each 50 mL of gel bed volume.

2. Use 1 g Sephadex G-25 per every 4-6 mL of bed volume. 50 g of
Sephadex will make 200—300 ml bed volume. Use twice the volume of
buffer as bed volume, place Sephadex in buffer and set aside to
swell. (Cover! Do not allow to dry.)

3. To prepare 200 mM (NH4)2804 use 0.246 g in 10 mL distilled water.

4. Mix Hemoglobin in a ratio of 5 mg/mL of 200 mM (NH4)2804. 5 mL of
this solution will be enough but 10 mL may be more practical for
dispensing.

5. To prepare the 200 mM 38C]: use 0.416 g of BaClz per every 10 mL
distilled water.

BACKGROUND_1NEQRMAILQN=

Gel permeation chromatography separates materials based strictly
on size. Charge and solubility of polar or nonpolar solvents has no
effect on these separations. In biochemical laboratories gel
permeation chromatography is commonly used to exchange the buffer or
salts in a protein solution, or used in the final stages of protein
purification to separate small protein molecules from large protein
molecules.

Using a gel permeation column is relatively easy but does require
attention to several details. These details are:

1. Particle (bead) size. The important point of particle size
is that the smaller the particle the larger the resistance
to solvent flow. 0n the other hand , the smaller particles
give better resolution (separations) than the larger
molecules. The smaller beads also have smaller pores to
“detour” the smaller molecules.

2. Fractionation range. The fractionation range indicates the
size of molecules that can pass through the matrix of the
media. Molecules that are too large cannot diffuse through
the matrix and therefore, are excluded.

3. Swelling time. Gel permeation media in the dry state
requires a finite time to take up water. The media with
large porosities take longer to swell. Heating, to 90° C,
can greatly decrease swelling time.

4. Maximum operating pressure. Because gel permeation media
are not rigid structures, exceeding the maximum operating
pressure will cause the media to collapse.

5. Bed volume. The bed volume allows one to calculate the
amount of dry media to weigh out to fill the column. By
using the formula 'Pi'r‘h the volume of the column can be
determined by measuring the inside diameter and height.

139

Dividing the column volume by the bed volume determines the
weight of the dried gel needed.

Columns may be reused after re-equilibrating with buffer. To
prevent microbial growth during storage, add an antimicrobial agent,
such as 0.02% sodium azide, to the equilibration buffer. The
antimicrobial agent may be eluted from the column before another run.
If you are planning on doing further investigations using molecules
that are close in size you will need a much longer column to get a
good separation.

W:
1. Tubes 4 & 5 and possibly 6. Tube 5 has the higher concentration.
2. Tubes 7 - 10, with 6 a possibility.

3. Tube 6. ( These answers are not necessarily restricted to these
tube #’s but are relative in the order of molecular separation.

4. Hemoglobin is the larger molecule. The larger molecules pass
through the column faster as the smaller molecules enter pores
between the beads and pass through more slowly.

5. The smaller the bead (particle) size the greater is the resistance
to the solvent flow and the better the resolution (separation) of
the collected molecules.

W:

1. Sephadex G-25-300 can be obtained from Sigma Chemical Company,
phone 1-800-325-3010. P.0. Box 14508, St. Louis Mo. 63178.
(Bio-Gel P—6, coarse, 50-100 mesh is an equivalent that is
available from Bio-Rad Lab, 32nd and Griffin, Richmond, Ca.)

2. The Trls HCL and Tris base for the buffer solutions are available
in many supply catalogs. ( Fisher, Carolina, and Sigma )

3. Hemoglobin (powder) is available from any biological supply
catalog.

140

GEL PERMEATION CHROMOTOGRAPHY

W:

Gel permeation chromatography separates molecules based strictly
on size. The charge and solubility of polar or nonpolar solvents has
no effect on the separation. In biochemical laboratories gel
permeation chromatography is commonly used to exchange the buffer or
salts in a protein solution, or in the final stages of a protein
purification to separate small proteins from large proteins.

Using a gel permeation column is relatively easy but does require
attention to several details. These details are: particle (bead)
size, fractionation range, swelling time, operating pressure, and bed
volume. (Your teacher may wish to discuss these with you.) In this
lab particle size is important to you. The smaller the particle size
the larger the resistance to solvent flow. The smaller spaces created
by smaller particles, as opposed to large spaces between large
particles, yield better resolution (separation). Therefore, the size
of the beads (particles) in the column determines the efficiency in
separating various sized molecules.

This laboratory exercise demonstrates the separation of
hemoglobin and ammonium sulfate by gel permeation chromatography. The
separation occurs as the molecules travel through layered beads. The
beads used for these columns are porous. As the mixture passes
through the column, the smaller molecules get “detoured” in these
pores and proceed down the column more slowly. The larger molecules
do not enter the pores and are carried along with the solvent, passing
out of the tube before the small molecules.

W3:

To separate small molecules from large molecules using gel
permeation chromatography.

To determine the order of molecular collection by using gel
permeation chromatography and spectrophotometry.

To explain how bead size affects the separation of molecules in
gel permeation chromatography.
W:

Be sure to maintain a liquid level above the column bed at all

times. 00 NOT ALLOW COLUMN TO GO DRY ii! The bed column would
collapse.

141

Wipe test tubes clean of fingerprints and smudges before placing
into Spec 20.

W:

Ammonium sulfate (NH4)2804

Barium chloride ( BaCla )

Hemoglobin ( 5 mg hemoglobin/mL of 200 mM (NH4)2304 )
Sephadex G-25 in buffered solution

Tris buffer ( 25 mM, pH 8.0 )

Column ( 25 cm x 10 mm ) or equivalent
Disposable syringe or funnel ( 50 cc or larger )
Rubber tubing ( 2 ) 10 cm and 30 cm lengths
Pinch clamps ( 2 )

Test tubes ( 10 ) 13 mm x 100 mm

Test tube rack

Spectrophotometer ( Spec 20 )

Ringstands ( 2 )

Buret clamps ( 2 )

Micropipette or equivalent

Marking pencil

Pipette ( 1 mL )

Dropper

Distilled water

0 DU
Part I Setting Up The Column

1. Place disposable syringe above column as the source for buffer
flow. Attach disposable syringe to highest point on ring stand
with buret~clamp. Attach the longer rubber tubing to the syringe
bottom: place pinch clamp on far end of tubing.

2. Attach column below syringe using buret clamp. Leave enough
clearance at base of column to draw off samples into test tubes.

Connect the shorter tubing to the bottom of column and place pinch
clamp on far end.

3. Be sure filter disc is in bottom of column. If gel permeation
columns are not available, a small cotton plug in the bottom of a
[buret works well as an alternate column.

4. Stir the Sephadex and slowly fill column. Allow the liquid to run
through column by opening pinch clamp. Continue stirring mixture
in beaker as you fill column to within 1-2 cm from top adapter.
Keep Sephadex bed covered with liquid at all times. (Do NOT allow
column to go dry).

142

Place two times the column’s volume of buffer into the syringe and
attach upper tubing to top of column. Open top pinch clamp and
allow two column volumes of buffer to flow through column (open
bottom clamp) to insure uniformity and stabilize bed. Close top
clamp and allow buffer level to drain to within 1 cm of column bed
and stop flow with bottom pinch clamp.

Part II Separating The Molecules

(Turn on the Spec 20, allowing it to warm up before beginning part

LI).

Carefully add 100 uL of the hemoglobin solution to the surface
(t0p) of the column bed. Solution must be added slowly so that
the surface of the bed is not disturbed. Open bottom pinch clamp
slowly and allow hemoglobin to Just enter bed and stop flow.

Gently add buffer to fill column and attach upper tubing. Put
more buffer into disposable syringe if needed. You will be
drawing off ten 1 mL samples.

Using a 1 mL pipette place 1 mL of distilled water into one of the
tubes and mark the surface level on the tube. Discard the water
and mark all remaining tubes at the same height.

Allow column to flow slowly and collect ten 1 mL column fractions
(samples).

Part III Analyzing The Fractions

1.

Add 1 drop of 200 mM BaClz to each tube. Record color change or
formation of precipitate.

Add 2 mL distilled water to each tube. Remove the level mark from
all test tubes.

Set Spec 20 to 450 nm and blank with distilled water. Insert each
of the ten tubes into the Spec 20 and record the percent
transmittance. Be sure to follow proper Spec 20 procedures and
wipe off tubes with a tissue to remove smudges or fingerprints
before inserting.

143

MW:

1.

Which tubes contain hemoglobin? Which tube has the higher
concentration?

Which tubes contain the precipitate Ba804?

Are there any tubes that contain both hemoglobin and the
precipitate? If so, which ones?

Which is the larger molecule, the hemoglobin or the ammonium
sulfate? Upon what information is your answer based?

Explain how bead size affects the separation of molecules in gel
permeation chromatography.

144

W:

Separate other small molecules from other large molecule, such as
hemoglobin and an indicator.

Separate proteins using much finer meshed beads.
Separate proteins in meats.

Separate hemoglobin and myoglobin.

W:

Suelter, C. S. 1987. “Biochemical Techniques - Chromatography“
Michigan State University

BI BLI OGRAPHY

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