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D OIL‘uv- . .l.‘. 1 .I l..\ 5...}: Iv \. 1 V l . . 2. 1.52.1... .. 333....-. .‘I as: Bul . . ..._ J .. r. . .v... Ix . ....,..r. .1. . .v "2,21... ..Pm.v 35...»; r12. .rwwkkmmlfbm} 6.. . $§E¥QM?&K~¢&EL£VMW£F "rdxfifi. .4. Emma rgwwwm..n§:é fiwwwflgrfuawnfirumk .§: I. I: c! 112. ..t..:....!.{rl.n7..!.l .2 .I. § :2 . .n. . ,2. . . .....uv. ..x.§l.II .nalliv. 13v..n......$.... I.» . .53 .r. .v . .. . . .1. IGAN TATE J'llllllllflwuuu arm ~ Minimumll K. 300 945094 This is to certify that the thesis entitled A LABORATORY CENTERED MOLECULAR BIOLOGY TEACHING MODULE TO FACILITATE LEARNING OF BIOLOGICAL SCIENCE presented by MICHAEL JAMES BRUNDAGE has been accepted towards fulfillment of the requirements for MASTER degree in SCIENCE Date 4999 %7/ £2 / q 0 f 0-7639 MS U is an Affirmative Action/Equal Opportunity Institution .._ __.. _ ____h___ __ _—__—_-_- __ —_—.‘ F “may fl “hum Cute 1 Unlvonlty L_ fl fi PLACE IN RETURN BOX to remove this checkout from your record. TO AVOID FINES return on or before date due. F—=_———__——.__——___————— DATE DUE DATE DUE DATE DUE A “‘p «l I l‘.‘\, I/r“ § J i:=E [__ ll T—lf usu Is An Affirmative Action/Equal Opportunity Institution CWMMR , 7M 7 . ._. _. _.——_ A LABORATORY CENTERED MOLECULAR BIOLOGY TEACHING MODULE WHICH FACILITATES THE TEACHING OF BIOLOGICAL SCIENCE By Michael James Brundage A THESIS Submitted to Michigan State University in partial fulfillment of the requirements for the degree of ' MASTER OF SCIENCE Interdepartmental Biological Science 1 990 ABSTRACT A LABORATORY CENTERED MOLECULAR BIOLOGY TEACHING MODULE TO FACILITATE LEARNING OF BIOLOGICAL SCIENCE By Michael James Brundage Students entering second year high school biology classes have diverse scientific backgrounds. Subject material including cytology, genetics, and physiology, necessitates an expanded knowledge base in molecular chemistry. To give all a somewhat equal starting point, a ten week molecular biology learning module initiates the class. The module, and its laboratory activities, are designed to develop knowledge of: atoms and molecules, chemical reactions, bioenergetics, pH and buffers, carbohydrates, lipids, and proteins. Analytical techniques introduced include: Ouchterlony Double Diffusion, spectrophotometry, gel permeation chromatography, and gel electrophoresis. Judgement of the success of the module is based upon clinical interviews, pre and post test scores, classroom discussions, and laboratory behavior. The motivational capacity of hands-on activities focuses student effort. This attention increases learning of the abstract lecture material. Students show increased dexterity with laboratory equipment during unstructured tasks. During the exit interviews, favorable attitudes toward science class are noted. ACKNOWLEDGEMENTS My heartfelt thanks goes to: Dr. Clarence H. Suelter, Dr. Howard H. Hagerman, and Dr Martin T. Hetherington, all members of my committee, for directing my academic development. I appreciate a special fellowship with the members of the 1988 M.S.U. summer research group: Mary Fowler, Van McWilliams, Marie Rediess, and Tammy Voss. I would like to commend the National Science Foundation, Michigan State University, and its staff for making this type of endeavor possible for teachers. I am grateful to my wife, Fran, and our daughter, Michelle for support of my efforts. GONNA CONCOU‘IJ \ICDOLh-k-hww \ImNV-komfl TABLE OF CONTENTS Body of Thesis Introduction Student Transformation Instruction Evaluation Conclusion Reference Pages Appendix A: Molecular Biology Item List Appendix B: Clinical Interview Appendix C: Examples of Handouts Appendix D: Daily Calendar Appendix E: Detailed Lesson Plans Appendix F: Quizzes Appendix GzTests References Cited .5. 4.; (D m-‘CO 19 20 LIST OF TABLES Table 1, Concepts and Real World Connections Table 2, Laboratory Exercise Placement Table 3, Student nterview: Vocabulary Item Anal sis Table 4, Percent 0 Students Scorin Within LAchievement Ranges With otal Word IS Table 5, Percent of Students Scoring Within Achievement Ranges With Laboratory Associated Terms Table 6, Tallied Laboratory Word List From Student Interview 31 31 32 32 UST OF FIGURES Figure 1, 1989 & 90 Pre-Test 2 Scores Figure 2, 1989 & 90 Post Test 2 scores Figure 3, 1989 Pre/Post Test Score Comparison Figure 4, 1990 Pre/Post Test Score Comparison INTRODUCTION STATEMENT OF THE PROBLEM Will the introduction of a ten week molecular biology teaching module to a second year high school biology class (1) accomplish the stated objectives (see p. 7), and (2) will it facilitate future conceptual development in cytology, genetics, and physiology? Will fulfillment of the objectives be influenced by adding laboratory investigations into the module? To understand modern biology, students need a working knowledge of chemistry. This work describes an integrated approach for teaching molecular biology to second year high school biology students with inclusion of several laboratory exercises, and its success in student motivation. According to Bybee & Landes (1990), "The nature of the activities and approaches must be such that students have time to explore ideas, become acquainted with scientific or technologic concepts, and have the opportunity to apply the new concepts and evaluate their adequacy.” LITERATURE Current literature suggests a trend toward increasing the involvement of high school science students in laboratory experiences or hands on activities. As stated by Okebukola (1985), ”There has recently been a noticeable increase in published biology laboratory activities that depend heavily upon engaging the student in manipulative experiences to discover concepts rather than to verify them”. Many of these materials contain complex procedures including the use of relatively modern research technologies. Though this may be a good idea, Gardner (1988) states that "While most educators agree that students should be exposed to the marvels of modern biology, teachers are concerned as to where such units will fit into an already overcrowded list of course objectives”. To alleviate this problem, the exercises ought to be designed to facilitate achievement of the objectives already in place, and, when possible, should reinforce concepts and ideas previously covered. In addition, if they develop concepts deemed important enough to be newly introduced, information gleaned from the investigations ought to be supported by material covered later in the course. Research about the format of laboratory exercises has led to the approbation of the Guided Inquiry laboratory approach. The Biological Sciences Curriculum Study, W Emma (1987) is a course plan which incorporates the Guided Inquiry method into investigations. It involves the formation of four sequential domains; introduction, materials, procedure, and discussion, each dealing with important segments of learning. The written introduction gives real world accounts of characteristics within the inquiry and explains its scientific goals. A materials list alerts the students to the exercise, equipment, and prior knowledge needed to operate it. The procedure is a series of carefully written steps which leads the student through the process. A key aspect of the Guided Inquiry procedure is the opportunity for students to engage in science processes. ”Frequently included are more difficult skills, such as identifying variables, controlling for and manipulating variables and quantifying data" (Ingelsrud & Leonard, 1988). The discussion section is composed of questions which relate to the interpretation of the data and attempt to mold the student's concept of the area being studied. Laboratory investigations published in the science teaching journals; 1mm, W. and W as well as those found in the newer copyrighted texts and lab manuals, use the Guided Inquiry format. Personal and colleague participation in recent National Science Foundation funded teachers' workshops report requests for the Guided Inquiry format when developing or altering laboratory investigations. CENTRAL QUESTIONS Many American high school students, are not very interested in taking science classes. If this is not true, why must two years of science be a W for graduation by most Michigan school districts? Flannery (1988) states, ”As every teacher knows, many students see science as difficult, complex and boring. Few, especially among nonscience majors, see it as interesting, illuminating and exciting”. Perhaps a class in general biology and introductory chemistry are as far as most want to delve. Many reasons may be cited as the cause for the apparent apathy, but lifeless lectures, boring group activities, and non-realistic classroom discussions are among the reasons. The vast heterogeneity of topics covered during elementary and middle school science education may also play a role. If high school students could have a standard knowledge base in science prior to entering high school, their teachers would know where to begin. Accordingly, if standards for graduation from high school were more explicit, teachers would know what to teach. With desire to teach for breadth rather than depth, teachers too often ”present” materials to students once, with the attitude that those who are interested will learn the material while those who do not learn it are not studying hard enough. Repeated use of the same teaching materials and methods does little to resolve the issue. If we want students to become more excited about science, we must develop laboratory activities which incorporate new technologies and real life situations. Robertson, (1989) has suggested that ”conceptual understanding is associated with connections «connections between science concepts and everyday life and connections among the different science concepts in a discipline.” To make the connections involves exploring "in place” classroom objectives, finding areas concerning students' problems, examining the texts and labs, interviewing pupils about their knowledge of and feelings for science classes, and then trying to make some reinforcing alterations. To begin this process, new laboratory exercises with introductions showing ”real life" connections need to be acquired. During the summers of 1987 and 1988, several modern molecular biology laboratory activities were developed by high school teachers attending workshops held on the campus of Michigan State University. Ten of these activities were chosen by teachers for their probable applicability within the present high school curriculum. The laboratory exercises were pre-tested by the teachers, to determine their feasibility in the high school science environment, and revised where needed. Some of these labs are incorporated into the molecular biology module. This is a report of student involvement with the module and subsequent assessments of their perceptions of biology and chemistry. OBJECTIVES Prior to the 1988/89 school year the second year program of biology in the Lapeer School District included studies in human anatomy and physiology. The predominant goal was ”to develop the students' knowledge of human anatomy and physiology.” The major laboratory exercises involved dissection of a preserved cat. Some molecular biology, cytology, and genetics were included in the initial phase of the course, but the depth of concern with these subjects was clearly inadequate. With the development and testing of laboratory exercises for a molecular biology module during the summers of 1987 and 1988, and the module's implementation during the school year of 1988-89, new aspects of cellular physiology were incorporated into the second revision of the class outline. The most recent schedule of subjects integrates technology and molecular biology with cytology, genetics, and physiology. Appendix A is a list of terms used to help evaluate the success of the teaching module. The list includes the key terms and concepts to be understood and processed by the students, and it conveys the depth of study during the module. The order of the list is as presented to the students during an exit interview. Two sets of objectives, one which guided the development and research of the laboratory exercises, and the other which was developed for teaching the module, were prepared and are listed below. RESEARCH PROJECT OBJECTIVES 1. To develop successful inquiry approach laboratory exercises for biology and chemistry classes. 2. To introduce scientific technology to teachers. 3. To learn places where laboratory experiments and exercises can be integrated into established curricula. 4. To increase teacher competence in aspects of molecular biology. TEACHING UNIT OBJECTIVES 1. To stimulate interest in molecular biology. 2. To prepare a knowledge base for further biological studies. 3. To introduce laboratory equipment and develop some dexterity with it. 4. To give practice with data collection, graphing, and interpretation. 5. To give practice at deductive reasoning. 6. To positively influence attitudes towards science classes 7. To correct and reinforce biological concepts 8. To cite examples of how science is connected to real world objects and systems. Development of an understanding of the kinetic molecular theory of matter in the minds of biology students is a good starting point. Knowledge in this area facilitates the learning of many natural phenomena. Prerequisites to understanding cellular metabolism are reaction kinetics and chemical bonding. Since living material has a composition high in water, information about solutions, concentrations, ionization, polarity, and pH is essential. The concept of compartmentation of the cell, and movements of materials to and from these compartments, requires knowledge of the molecular organization of cell membranes. Knowing structure and function of carbohydrates, lipids, proteins, and nucleic acids is necessary if students are to deal adequately with genetics, cytology, and physiology. Few, if any, areas of biology can be well understood without some knowledge of biochemistry. Student objective two is to broaden the knowledge base of biochemistry. Cognition, the result of learning experiences, can occur at various levels. Bybee & Landes, (1990) indicate ”that learners actively construct a world view based on their observations and experiences.” Student misconceptions derived during primary development of a perception can cause flaws with future thinking. Immature students may misinterpret information regardless of source. If teachers present biology as an inquiry rather than a series of facts, perhaps students would feel less defeated and would begin to see science more realistically. Investigative experiences concerning concept areas with which the students are to become familiar seem to enhance perception and attitude. In addition, connecting scientific concepts with real world situations can aid student comprehension. Throughout the teaching effort tied to this thesis, connections and analogies between the real world and concepts being studied are identified. (Table 1) Table 1, Concepts and Real World Connections CONCEPT BEING STUDIED REAL WORLD CONNEC'RON HEWGLOBN WLECULE SICKLE CELL ANEMIA DISULFDE ENDS CURLED HAIR pH SHAMPOO/ACID RAIN INDICATORS URINALYSIS TESTS PFDTEIN DENATURATION FRED EGGSAERINGUE CARBOHYDRATES NUTRITION LIPIDS NUTRITION PFDTEINS NUTRITION MEDIATED TRANSPORT DRIVER/FAST FOOD WINDOWS LIPIDS/EMULS IONS VINEGAR AND OII. DRESSING POLYMERIZATION POP-BEADS BETA- PLEATED SHEET FOLDED PAPER FAN CATALYST SET UP FIGHT/BOY AND GIRLFRIEND ENEmYTRANSFER A DAM/TURBINE, GENERATOR ANTENNA CHLOROPHYL RADIO/TV ANTENNAE HELIX SLINKY H—BONDING ICE CRYSTALS/SURFACE TENSION HYDROGENATED Ol MARGARINE BU'IYRIC ACID BUTTERMILK/BUTTERSCOTCH HYDFDPHOBC HYDROPHOBIA/CLAUSTROPHOBIA GUESTERG. GALL STONES/STROKE/BLOOD P. The laboratory exercises, which were tested and rewritten during the summer research session in 1988, are presently being used in an attempt to increase interest and cognition in the four major content areas of the second year biology class. The laboratory exercises and their current arrangement in the module 10 are listed in Table 2. Complete copies of the exercises are located at the lnstructural Software Collection in the Michigan State University Library. 11 Table 2, Laboratory Exercise Placement NAME OF LAB EQUIPMENT INTRODUCED PLACEMENT Ouchterlony Diffusion aspirator Atoms and Using Salt Solutions agarose gel molecules micropipettes Introduction to spectrophotometer Bonding and Spectrophotometry reactions Separation of Hemoglobin Sephadex from Ammonium Sulfate gel chromatography columns Using Gel Permeation pH indicator sticks Molecular Chromatography indicator mass various pipette types/pi-pump spectrophotometer Biological Materials pH indicator sticks pH and buffers as pH Indicators Pasteur pipettes General Effect indicators of Salivary Amylase Pasteur pipettes Proteins and On Starch spectrophotometer enzymes Coagulation Temperature melting point tubes Enzymes and of Chicken Egg White pH indicator sticks denaturation Pasteur pipettes Concentrations of Protein indicator Standard curve in Saliva Using Biuret Solution volumetric pipettes/pi-pumps Concentration spectrophotometer Protein Digest By Papain pH indicator sticks Enzymes and Bromelain electrophoresis apparatus Electrophoresis of pH indicator sticks Buffers and Protein agarose gel, stain/destain protein various pipette types During the ten week module the time alloted for atomic and molecular theory of matter is about two weeks. Atomic and molecular theory of matter are taught through lecture, discussion and involve worksheets. 12 Beginning with the Bohr model of the atom, the students work through charge, number, and location of sub-atomic particles. The idea of atomic mass and molecular weight are next in the sequence; introduction of quantum numbers and electron configuration sum up the time used to study the atom. After this ionization, and ionic, covalent, and hydrogen bonding are discussed. The introductory Ouchterlony Double Difusian exercise is used to demonstrate ionization of salt compounds in solution, their ability to diffuse through a gel substrate, and their capacity to recombine with other ions. The Ouchterlony investigation facilitates understanding the concept of gel electrophoresis of proteins and gel permeation chromatography which are incorporated later in the module. An introductory spectraphatametric laboratory exercise occurs during this section, and study of Beer's law reinforces the concept of the molecular nature of matter. Studies in molecular polarity strengthen knowledge of electrically charged particles. Combination, decomposition, and single/double replacement reactions are covered at this point and are of great importance to later understanding of metabolism. Gel permeation technology is discussed and an exercise in hemoglobin from ammonium sulfate separation follows. Molecular and ionic kinetics is extremely important to understanding movement of molecules across membranes. Passive diffusion, facilitated diffusion, and various forms of mediated transport can only be accurately understood when one has a strong basic knowledge of the physical characteristics of matter. 13 Structure, banding, bioenergetics including exerganic/endergonic reactions, free energy, coupling and energy transfer are needed ideas for conceptual development of cellular activity. The Walt Disney Studios produced film, Worn, is used in conclusion. Once these areas are understood shifting to the study of energy transfer within living systems occurs more readily. The fact that chemical reactions occur in living cells, and that they only happen if the energy situation is favorable, appears to be new to the students. They do not seem to think of living organisms as ”chemically active conglomerates” working in coordinated fashion. During first year biology classes, most teachers devote many hours to explanations describing energy relationships in living processes. They talk of the sun powering the whole system, producers harnessing the energy and making some of it available for the consumers. Discussions of photosynthesis and cellular respiration came afterwards, attempting to express the concept of energy transfer, but to little avail. This is because many students do not understand the comparative size and arrangements of molecules making up the cell organelles. Many also lack a general knowledge of the characteristics of energy. For example, let us examine the following two sentences. ”The electrons travel from cytochrome to cytochrome, giving up some of their energy to enzyme molecules called ATP synthetase. These molecules are found in the membrane surrounding the mitochondrial matrix and form ATP from ADP and phosphate." In order for an eleventh grade student to understand, one must insure 14 the student has cognition of the molecular nature of the mitochondrion, and has same concept of free energy, coupling, and energy transfer. Perhaps chemistry and physics ought to be pre- requisites for biology. Most high school biology laboratories will have: beakers, flasks, graduated cylinders, eye-droppers, dissecting tools, filter funnels, mortar and pestle, paper chromatography chambers, and microscopes. However, high school laboratories where molecular biology Is taught require that the list be expanded to include: Pastuer, volumetric, and micropipettes, Pi-pumps, a centrifuge, Ouchterlony plates, spectrophotometers, gel permeation columns, thin layer chromatography plates, affinity chromatography columns, gel electrophoresis apparatus, and melting point tubes. Student comments when asked, " With which laboratory equipment, instruments, and processes have you developed some dexterity?", consistently choose use of the spectrophotometer and pipetting. Time restraints often interfere with the exercises involving use of electrophoresis equipment, thus various levels of proficiency with this apparatus occur. STUDENT TRANSFORMATION 15 16 CLINICAL INTERVIEW To help judge if the stated teaching objectives have been met, a clinical interview is held with each of twelve students over the two year study. The questions asked during the hour long discussions are listed in Appendix 8. Students are selected to be interviewed according to their final class standing. Two students with highest and lowest percentage of accumulated points, as well as two students in the middle of the range, are chosen, and intensively interviewed at the end of each year. The questionnaire is divided into two portions. The first is a covert attempt to see if the students know that a basic back -ground in molecular biology is necessary for understanding biological concepts. Answers to questions designed to test the hypothesis (see Appendix B, questions 4, 5, 7, 12, and16) confirm that they do. At the same time the questionnaire queries the students as to their feelings about the laboratory exercises. The second part of the questionnaire is a list of terms and procedures with which the students ought to have become familiar during the course. All items on the list are introduced during the molecular biology module and many of them are actively used throughout the school year. During this section of the interview the student is asked to make an open statement about his or her understanding of each term. The interviewer, using subjective judgement, tallies the students' responses as excellent, good, or poor. (Table 3). The expected outcome would be that the ones scoring the highest on the pre-test would understand more. (See Tables 4 & 5) 17 However, the list is prepared so it can be used to determine if the lab exercises have a positive effect on learning and retention. Of the seventy-seven terms included in the list, twenty -one are involved with the laboratory exercises. Table 6 summarizes the number of times items associated with laboratory are well understood. Twenty-one of the seventy-seven terms (22%) show strong evidence of retention. (see table 3) Nine of these twenty-one (43%) were introduced during laboratory time and twelve of fifty-six (21%) during lectures. A Chi square test done with this data (which shows a less than 30% probability that the difference occurs due to chance) may be used as evidence that the exercises increase retention of terms. 18 Table 3. Student Interview: Vocabulary Item Analysis (4-) = excellent, (-) = good, (O)= poor map + - 0 WORD + - 0 WORD -I- - 0 ABSORBANCE 12 0 0 HYDROPHILIC 12 0 0 AMPHIPATHIC 8 4 O KINASE 10 2 0 CARBOXYLASE 10 2 0 PHOSPHORYLASE 6 6 0 TERTIARY 6 2 4 QUATERNARY 1O 2 O MERISM 10 2 0 DISSOCATION 6 4 2 POLAR 12 O 0 NON-POLAR 12 0 O PERMEATION 8 2 2 SPECTROPHOTOMETER 10 2 O ENDERGONIC 10 0 2 TRANSMITTANCE 8 2 2 EXERGONIC 10 0 2 COVALENT BOND 8 2 2 BUFFER 8 4 0 IONIC BOND 8 4 O OLIGOSACCHARIDE 10 2 0 DISULFIDE BOND 10 2 0 KETOSE 6 2 4 TRIACYLGLYCEROL 4 6 2 ALDOSE 6 4 1 ALANINE 10 0 2 GLYCINE 6 0 6 PHOSPHOLIPID 6 2 4 HYDROGEN BOND 0 8 4 TRYPTOPHAN 6 0 6 CYSTEINE 6 O 6 METHIONINE 10 0 2 MELTING PT. TEMP. 6 2 4 PEPTIDE BOND 10 0 2 CATALYST 12 0 0 WAVELENGTH 12 O 0 LIGAND 8 2 2 NANOMETER 8 2 2 SEPHADEX 12 0 O ELECTROPHORESIS 12 O O AGROSE 8 2 2 BEER‘S LAW 8 0 4 PIPE'ITE 12 0 O OUCHTERLONY 12 O O REDUCE 8 2 2 LAMBERT'S LAW 10 4 O OXIDIZE 4 4 4 EMP. FORMULA 10 2 0 DALTONS 8 4 O MOLE 4 8 0 COMB. REACTION 1O 0 2 STRUCT. FORMULA 12 0 O ELECTRON DOT FORM. 10 2 0 DBL REPLACEMENT 12 O 0 FREE ENERGY O 4 8 SINGLE REPLACEMENT 10 O 2 ANION 4 2 6 ASPIRATOR 2 0 10 CATION 4 2 6 EXTRAPOLATE 12 0 0 INTERPOLATE 12 0 0 PRECIPITAN LINE 8 O 4 PHOTOMETRY 2 2 8 LOGARITHM 6 6 0 EXTRACT 12 0 0 ALBUMIN 10 2 C COOMASSIE BLUE 6 4 2 AMYLASE 10 2 0 INDICATOR 10 2 O CENTRIFUGE 12 O O DESTAIN 8 0 4 PARAFILM 12 O O GLYCOLIPID 6 4 2 CENTRIFUGAL FRACT. 2 4 6 GLYCOSYLATION 4 0 8 DECANT 4 0 8 GLYCOPROTEIN 10 0 2 19 Table 4, Percent Of Students Scoring Within Achievement Ranges With Total Word List High achiever - "A” student, Medium achiever - "C" student, Low achiever - 'E" student STlDBVTCATEGORY STUDENT UNDERSTANDING OF ITEM °/o EXCELLENT % GOOD % POOR HIGH ACHIEVER 82 10 8 MEDIUM ACHIEVER 72 15 13 LOW ACHIEVER 53 19 28 Table 5, Percent Of Students Scoring Within Achievement Ranges With Laboratory Associated Terms High achiever - "A” student, Medium achiever - ”C" student, Low achiever - "E" student STIDBVT CATEGORY STUDENT UNDERSTANDING OF ITEM °/o EXCELLENT % GOOD °/o POOR HIGH ACHIEVEMENT 98 0 2 MEDIUM ACHIEVEMENT 69 12 19 LOW ACHIEVEMENT 62 14 24 20 Table 6, Tallied Lab Word List From Interview LIST ITEM # OF STUDENTS UNDERSTANDING ITEM EXCELLENT (+) GOOD (-) POOR (0) TRANSMITTANCE 8 2 2 REFER 8 4 0 W86 1 2 0 O PIPETTE 1 2 0 0 LAMBERTS LAW 1 0 2 0 ASPIRATOR 2 0 1 0 COOMASSIE BLUE 6 4 2 m 1 2 0 0 DECANT 4 0 8 SPECTFDPHOTGEI'ER 1 O 2 O W 1 2 0 O PRICIPITIN LINE 8 O 4 EXTRACT 1 2 0 0 DESTAIN 8 0 4 ABSORBANCE 1 2 0 0 MELTING POINT TUBE 6 2 4 WAVELB‘IGTH 1 2 0 O SEPHADEX 1 2 0 0 BEER'S LAW 8 O 4 NDICATOR 1 O 2 0 PARAFILM 1 2 0 0 21 LITERATURE ANALYSIS A textbook has not been chosen for the second year biology course. A multiple text approach was deemed most acceptable by the school district prior to inception of the class. Classroom sets of Jacob 8: Francanne (1982), and Vander et al (1980), were purchased as references. Lack of a textbook, and the fact that the class was originally organized to teach only human anatomy and physiology, forced production and distribution of copies of sections from Metcalfe's et al (1986) teacher's resource notebook. This material is used in conjunction with the beginning chapters of the classroom resource texts, W W and W. These textbooks include basic explanations of: atoms, molecules, ions, polarity, solubility, concentration, and structural characteristics of carbohydrate, lipid, and protein molecules. The ten week molecular biology module allows expanded study of these areas and the addition of pH, buffers, catalysts, and reaction kinetics. The inclusion of the new material demands the availability of more information. This is provided by the teacher through lectures and handouts (Appendix C). Sources for these materials include Albert et al (1983), the October 1985 issue of Scientific American, Srere and Estabrook (1978), Barrett et al (1986), Ferdinand 1976, Dickerson and Geis (1969), Lehninger (1970), and Stryer (1981) as well as others. Since many of these resources are current they are assumed ”up to date” and correct. Objectives two, seven, and eight of the module, enhancement of the knowledge base, correction and reinforcement of biological 22 concepts, and real world connections are considerably influenced by the literature, lectures, and handouts. The other five teaching objectives are also impacted. INSTRUCTION 23 24 DAILY CALENDER The methods of instruction are varied and include lecture/demonstration, laboratory exercises, independent research, cooperative learning, films, monitoring tests, quizzes, worksheets, and reading assignments. To summarize the daily calender (see Appendix D), twenty five of the forty four days are used for lecturing and discussion, and thirteen days are spent in the lab. Six days are used in: conjunction with either films, reviews, or tests. LESSON PLANS A complete compilation of the lesson plans used to teach this module are presented as Appendix E. The four sequences include subject material, instructions to the teacher, examples for use by the teacher, diagrams to be drawn on the board, questions to the students, when to hand out copied materials, and when the quizzes (Appendix F) and tests (Appendix G) are to be administered. The lesson plans, by no means, are all inclusive. In order to teach the material a working knowledge of biochemistry is required. The labs which are incorporated into the module do not need exact placement, and therefore, are not positioned in the time frame. As is indicated earlier (Table 2), the labs are effective if placed within particular areas of study. A teacher wishing to implement the labs can rest assured that they are applicable to many areas of biology. It should be noted that the labs (Table 2) may involve the use of elaborate equipment, some of it is 25 expensive (A new spectrophotometer, $1,200.00). Teachers wishing to incorporate any of these labs ought to become familiar with them prior to use in the classroom. LABORATORY EXERCISES Student objective three is to introduce laboratory equipment, and have students gain some dexterity with techniques necessary for its use. This segment of the module provides great impetus for influencing attitudes towards the scientific endeavor. Student excitement, enthusiasm, and debate over proper use of equipment is evident during lab periods. Lab reports, including data tables, graphs where appropriate, written interpretations, and conclusions, generally exhibit extensive effort. The initial laboratory involves the use of Ouchterlony double diffusion to show how ions migrate through a colloidal phase of matter. It necessitates development of skilled use of an aspirator and micropipettes. Prior to the next laboratory exercise, a day is taken to discuss properties of light, and demonstrate how a spectrophotometer functions. The exercise itself involves an introduction to spectrophotometry, and with it successful student use of a spectrophotometer. ”Biological Materials as pH Indicators" is a lab which involves the preparation of extracts from pigmented portions of plants, and tests to determine if they are good indicators of pH. Students use Pasteur pipettes, pH indicator paper, and spot plates. If a fair number of extracts (5-8) are prepared, data collection necessitates careful consideration. As in all the labs, interpretation of the data is necessary to 26 answer the discussion questions at the end. During the section on proteins five investigations ensue. Each introduces new equipment such as melting point tubes and gel electrophoresis apparatus, and demands student involvement. Reinforcement of techniques already initiated includes the use of Pipumps and various types of pipettes, pH indicator paper (a pH meter, if available), and spectrophotometers. After the students have developed some functional skill with the apparatus, an open-ended assignment is given. The students are asked to develop a method for determining the number of pigments in plant leaves. They are allowed to gather their own leaves, prepare their analytical protocol, run the experiment, and do the research necessary to verify their conclusions. During the experimentation they use techniques such as thin layer chromatography, extraction, pipetting. and spectrophotometry. The most serious student effort, within the time frame of the module, occurs here. EVALUATION 27 28 STATISTICS Evaluation of academic achievement can be a difficult task. Some students perform best on objective tests, some on short answers, and others essay. Individuals can be sick or anxious when being evaluated. Because teachers are required to assign grades, we must make the best of a poor situation. Within the molecular biology module, numerous evaluation instruments are used to determine achievement. Positive student attitude and success on structured tasks, demonstrate a valid argument for the incorporation of modern molecular biology laboratory investigations into the teaching module. A carefully planned objective test, one which is dedicated to not only testing memorization and conceptual development, but also reasoning skills, may be able to measure realization of established goals. In conjunction, a well planned clinical interview can lend insight into intellectual development. The developed pre and post objective type test ( Appendix G) are one in the same. The test includes forty multiple choice items, and ten structural diagrams to be identified. The molecular diagrams are presented to the students from the blackboard, and vary, slightly, from pre to post test. Nine of the multiple choice items involve interpretation of presented data (questions 11-13, 16-18, 29-31). Of those, three (29-31) demand that students decide whether proffered conclusions are representative of the data. The Pre-Test is administered the first regular day of class, and the Post Test on the last day of the first quarter. After completion of the Pro-Test, students are informed that a similar 29 test will occur at the conclusion of the module to check for improvement. On day fifteen a major test (see Appendix G) covering, roughly, the first third of the module occurs. Thirteen five point quizzes (Appendix F) are given throughout the module, and are used as monitoring devices. Analysis of the pre-test raw data indicates a significant lack of knowledge about molecular biology. The mean i514, and the standard deviation is 4.32. Standard 2 scores (Figure 1) reveal 76% of the students score within one standard deviation while 94% are within two. Appraisal of the post test raw data shows a mean 33.16, and the standard deviation as 5.58. Standardized post test data (Figure 2) indicates 72% of the students score within one standard deviation, and 96% score within two. A t-score of 19.13 indicates a significant change has occured. Post test data exhibit an average point increase of 38% over pre-test scores (Figures 3 & 4). The least individual achievement is indicated by an 18% increase (9 points), while the greatest improvement is 64% (32 points). The correlation coefficient of two years of combined data for the pre and post test scores is .63. With a df of 48 the Null Hypothesis can be rejected with 99% certainty. A generalization claiming that the average 38% difference between the pre and post test scores may be due to the molecular biology teaching module can be made. Most students put forth strong effort during this module and the increase in the mean score of the post test may signify this. 30 Those few students showing little gain can be classified as intelligent ”problem children” who are placed into the class because of strong teacher discipline or those who pay little attention to counselors advice. The attempt to normalize student understanding of the chemical nature of living matter seems to be successful and this allows a more significant study of life processes for each. E OF STWENTS Figure 1, B 0" STWIENTS Figure 2, 1.8.0" 2.0“ 8.W " 4.00-I 0.00 - 31 -—————_~ zsconzs mean score (14), standard deviation (4.32) 1989 & 90 Pre-Test 2 Scores 20.0 J l I a 3 ascents mean score (33.16), standard deviation (5.58) 1989 8. 90 Post Test 2 scores 32 COIIKCT AIIHEIS Figure 3, 1989 Pre/post Test Score Comparison CORRECT ANSWERS Ian-rm Ire-1w Figure 4, 1990 Pro/post Test Score Comparison CONCLUSION 33 34 SUMMARY The inclusion of this module into the initial phase of a second year biology class profoundly facilitates students‘ ability to understand cytology, genetics, and physiology. The expansion of their knowledge of molecular biology increases the depth to which the other subjects can be studied. The lab activities involve the students in situations resembling actual scientific research. This, in turn, motivates positive attitudes for science, and reinforces newly developed concepts. STRENGTHS Active participation is the major key in education. The laboratory activities, as measured by the Chi square test and pre/post test scores are evidence of its success. During lab time the usual preoccupation with ”socialization" is at a minimum. Students are motivated by the challange of the endeavor, and this keeps their minds focused on what they are doing. At present, the molecular biology module includes much more lab time than do the other three modules making up the class. When asked for a comparison of preferred amounts of lab time, fifty percent of those students interviewed suggest more time be spent in the lab, and fifty percent feel the time devoted during the molecular biology module is about right. Development of student realization that a background in molecular biology is necessary for understanding other biological concepts is another strength of the module. The cytology module involves the study of membrane structure and function. Without 35 knowledge of phospholipids and proteins, and their inherent physical and chemical characteristics, accurate portrayal of mechanisms which move material through cell membranes is unlikely. One hundred percent of the students interviewed appreciate the importance of chemistry to cognizance of biological concepts. WEAKNESSES The most ”glaring" weakness of the module involves time restraints put upon the lab activities. Even though the labs are designed to be completed in an hour, or multiples of hours, they run over. Students rush to complete some sections, leading to frustration. Most teachers comply with requests for ”ten minutes” of their class time, but this puts a burden on them as well as their pupils. Students quickly realize that prior reading of the lab protocol, and prompt initiation of it, facilitates completion of the lab on time. A alternative might be to schedule two hour blocks of laboratory time into the day once or twice a week. SUGGESTIONS A high school level text, which includes all the material covered in the molecular biology module, would be of great value. Providing current reading information for the students becomes tedious and time consuming. Martini (1989) is the Lapeer School District's newly adopted text for the Biology II classes. It includes more of the chemistry information than previously used 36 classroom reference texts, but is still incomplete. A short textbook, written at tenth grade reading level, would be superior. The positive influence of a knowledge base in molecular biology, andgthe stimulation of student appetite through the use of labs involving modern research techniques, are fueling the development and alteration in other subject areas. Modules being affected include cytology and genetics. The genetics module embodies a new electrophoresis lab, and the cytology module entails labs involving electrophoresis, tissue culture, thin layer chromatography, and measurement of rates of cellular respiration. As time and money permit, new labs shall continue to be added. Perhaps the realization that cognizance of concepts and techniques in the field of chemistry are a prerequisite to comprehension of biology will alter the order in which the two subjects are presented. APPENDICES APPENDIX A MOLECULAR BIOLOGY ITEM LIST <‘.I. .“ I .5.\x Iv 37 MOLECULAR BIOLOGY ITEM LIST ABSORBANCE HYDROPHILIC AMPHIPATHIC KINASE CARBOXYLASE PHOSPHORYLASE TERTIARY QUATERNARY MERISM DISSOCATION POLAR NON-POLAR PERMEATION SPECTROPHOTOMETER ENDERGONIC TRANSMITTANCE EXERGONIC COVALENT BOND BUFFER IONIC BOND OLIGOSACCHARIDE DISULFIDE BOND KETOSE TRIACYLGLYCEROL ALDOSE ALANINE GLYCINE PHOSPHOLIPID HYDROGEN BOND TRYPTOPHAN CYSTEINE METHIONINE MELTING PT. TEMP. PEPTIDE BOND CATALYST WAVELENGTH LIGAND NANOMETER SEPHADEX ELECTROPHORESIS AGROSE BEER'S LAW PIPETTE OUCHTERLONY REDUCE LAMBERT'S LAW OXIDIZE EMP. FORMULA DALTONS MOLE COMB. REACTION STRUCT. FORMULA ELECTRON DOT FORM. DBL. REPLACEMENT FREE ENERGY ASPIRATOR CATION INTERPOLATE PRECIPITAN LINE LOGARITHM EXTRACT COOMASSIE BLUE AMYLASE CENTRIFUGE DESTAIN GLYCOLIPID CENTRIFUGAL FRACT. DECANT GLYCOPROTEIN SINGLE REPLACEMENT ANION EXTRAPOLATE PHOTOM ETRY ALBUMIN INDICATOR PARAFILM GLYCOSYLATION APPENDIX B CLINICAL INTERVIEW 38 CLINICAL INTERVIEW Which of the four areas of study this year was most interesting? A. Molecular biology B. Human genetics/Bioethics C. Cytology D. Human anatomy & physiology Which of the four areas was the most enjoyable/fun? Tell me something you remember from. each major unit. Make the comment about something you thInk IS Important. A. B. C. D. In what sequence do you feel the four _major areas should be studied, to best faCIIItate understandlng how organIsms work? Sequence the levels .of organization in the living world with the simplest first. ExplaIn what you can about how these levels are influence other levels. Arrange the levels in the order you know them with best first. Explain why you need to understand molecular biology in order to understand: genefics- cytology- A and P- Which specific areas of each major sub'ect is least understood by you? (Show them the outlines of eac module.) 39 9. Which laboratory experiences seemed most valuable to your understanding of the area being studIed? 10. Name and explain some cellular level functions of specific molecules. 11. How many methods of molecular transport can you name and describe? Describe them. 12. Tell me dyour concept of the Cell theory. Which area of those IIIt'Udtil? wguld necessarily have to be known to best understand IS eory. 13. Whichocomponent of the Cell theory do you understand best? eas . 14. Give an example of a homeostatic mechanism in a living organism. 15. Give Ian example of a specific metabolism and explain it SImp y. 16. Which are“? of study need(s) to be understood to better comprehen this mechanism and metabolism? 17. Give some examples of how comprehension in each _of the four areas studIed may be Important In your every day IIIB. molecular biology- genefics- cytology- A and P- 18. With which laboratory instrument/equipment/process have you developed some dexterity? 19. Is an hour sufficient lab time to complete most investigations? If not, WhICI'I ones seem to long? Where might the prob em lie? 20. Would you enjoy more or less laboratory work? APPENDIX C EXAMPLES OF HANDOUTS a ._I 40 EXAMPLES OF HANDOUTS OXIDATION-REDUCTION AND IONIC BONDING . Does the following equation represent an oxidation or a reduction of an atom of potassium? Prepare a sentence which explains your choice. K + bondenergy yields K’r + e‘ 2. Does the following equation represent the result of an oxmation or reduction? Prepare a sentence which explains your choice. Br- . In the following equation, which element has been oxidized and which has been reduced? Prepare a sentence which explains your choice. Mg + Br2 yields MgBrz OXIDIZED REDUCED . Diagram an electron dot formula for the following atoms. MEQBEIIILA Be atomic“r 4 atomic mass 9.0122 AI atomic‘ l3 atomic mass 26.9815 0 atomic" 8 atomic mass I5.9994 Using electron dot formulas, prepare an equation which illustrates ionic bonding between Li (Lithium) and 0 (Oxygen). Prepare a sentence which explains the equation and why it is correct. EQUATION- . Do the same as above for Mg (Magnesium) and Br (Bromine). Use the back of the sheet for your answers. 41 v.0: $.01 N..- AI 86% 05.325 IIII'. NO to 825 5:08“: m6 6 m6 0.. 42 BOND ENERGY Using the terms exerganic and endergonic. label the following reactions. A. I mole Na + 119 kcal 113195 I mole Na* + I mole e‘ B. I mole of Cl + I mole e' yield: I mole of Cl’ + 83 kcal C. I mole Na + I mole CI ylgigs I mole NaTCI' + 153 kcal D. 1/2 mole of "2 + 52 kcal ,1Lglgs I mole H E. I mole Mg + energy xlglgg I mole tig‘M + 2 moles e’ F. I mole Ng** + 2 moles Br' xlglg: 1 mole NgTTBr‘z + 587 kcal Complete each sentence with your own words. An exerganic reaction is one which An endergonic reaction is one which If we react two compounds in a beaker. and the beaker is warm after the reaction is complete. the reaction was . If we react two compounds in a test tube. and when the reaction is complete the test tube feels cold. the reaction was 43 ‘ Testosterone Cholesterol (3 male hormone) H CH3 GEEK/51c?“ I \CH. Vitamin D; Figure 3—5. Three common steroids. Questions Identify each of the following substances as: A. neutral lipids, 8. phospho- lipids, C. steroids, or D. waxes. 1. CH,(CH;);.—E—O—(CH;),.CH3 2. 0‘ / , O 3. H O 4. H C“) II H—é—O—C—R H—C—O—g-(CHMJI-ICHCHMH; I H— —O—C—(CH;)7CH-CHCH3CH-CH(CH1).CH3 H— | -O—$-(CH;)7CH-CH(CH;)7CH3 H O II H-é—o—g-CISHJI II H— —O--C—CIIH23 H- .0—E—CI3H27 I H O APPENDIX D DAILY CALENDER 44 DAILY CALENDAR Day 1 Discussion of section of school rules,_ introduction to teacher, subject material to be covered, location of eqUIpmrnt Day 2 Pre-test Day 3 Atomic structure, periodic chart, sub-atomic particles, symbols of elements, Ions, molecules Day 4 (Quiz 1) Ionic bonding, moles, bond energy, quantum theory, electron dot formu a, empirical formula Day 5 Movie: W Walt Disney Studios Day 6 (Quiz 2) Lab-Ouchterlony Diffusion Using Salt Solutions (set- up and preface) Day 7 Ouchterlony lab/Discussion of lab results Day 8 Covalent bonding, diatomic molecules, structural formula, nuclear fusion, valence, endergonic/exergonic Day9 . . (QUIZ 3) Lab eqmpment, spectrophotometry, graphing Day 10 Lab-Introduction To Spectrophotometry Day 11 (Quiz 4) Discussion of lab, hydrogen/disulfide bonding, charge polarity, general reactions types, free energy Day 12 (Quiz 5) pH/buffers, introduction of pH lab Day 13 Lab-Biological Materials As pH Indicators Day 14 (Quiz 6) Discussion of lab, Day 15 Test 45 Day 16 Introduction of organic molecules/structural vs functional, carbohydrates Day 17 (Quiz 7) Carbohydrates Day 18 Carbohydrates Day 19 Carbohydrates Day 20 (Quiz 8) Proteins Day 21 (Quiz 9) Proteins Day 22 Movie-Sickle Cell Anemia (N.I.H) Day 23. . . . Discussmn of mowe, reVIew Day 24 Protein, introduction of next lab Day 25 Lab-General Effect Of Salivary Amylase On Starch Day 26 (Quiz 10) Discussion of lab, introduction of next lab Day 27 Lab-Coagulation Temperature of Chicken Egg White Day 28 . Enzymes, catalysts, denaturation Day 29 _ . Envrronmental effects on enzymes, metabolism, ligands Day 30 (Quiz 11).Standard curves/concentration vs transmission, introduction of lab Day 31 Determining Concentrations of Proteins In Saliva Using Biuret Solution 46 Day 32 Discussion of lab, Introduction of next lab/set-up lab Day 33 . Lab-Protein Digest By Papain And Bromelain Day 34 Discussion of lab, lipids Day 35 (Quiz 12) Lipids Day 36 Lipids Day 37 Electrophoresis discussion Day 38 Preparing buffers, pK, sigmoid curve Day 39 (Quiz 13) Introduction to next lab, preparation of buffers Day 40 Lab-Electrophoresis of Proteins Day 41 Discussion of lab, review for test Day 42 Test Day 43 Review for major test Day 44 Post-test APPENDIX E DETAILED LESSON PLANS 47 DETAILED LESSON PLANS LESSON PLANS: ATOMS, MOLECULES, REACTIONS, ENERGY, pH AND BUFFERS Hand out periodic chart to each student Discuss chart, atoms, sub-atomic particles, how to determine the numbers of each, Bohr model, energy levels and quanta. They must know symbols for major elements found in living organisms: O, C, N, H, P, S, Na, K, Mg, Ca, Cl, Mn, Fe, Co, Cu, Zn 5 most abundant in universe: H, He, C, N, O H, C, N, O - 99% total mass of most organisms Define atom; smallest chemical unit of a substance that is capable of stable independent existence. - Ionic Bonding Discuss compounds and molecules Demonstrate ionic bonding of Na and Cl on the board show ionization of Na and Cl, explain how they become ions. (mole) (mole) (mole) ist 1 mass Na atoms + 119 kcal yields 1 mass Na ions + 1 mass 9 2nd 1 mass Cl atoms + 1 mass e yields 1 mass Cl ions + 83 kcal 3rd 1 mass Na ions + 1 mass Cl ions yields 1 mass NaCl + 189 kcal Discuss energy situation; 189 kcal + 83 kcal - 119 kcal a total gain of 153 kcal/mass (mole) Work other examples. For instance Mg + Br or Li + 0 Explain oxidized(lose electrons) and reduced(gained electrons) Work on developing concept by asking about what an oxidizing or reducing agent will do to an atom. Explain cations (+) and anions (-) -Covalent Bonding No transfer of electrons, shared instead Diatomic atoms; H, O, N, Fl, Cl Example 48 H + H yields H2 Electron dot formula H:H Structural formula H-H Empirical formula H2 2 masses H atoms yields 1 mass H2 molecules + 104 kcal aid 1 mass H2 molecules + 104 kcal yields 2 masses H atoms Have them explain the difference in their own written words. 104 kcal - BOND ENERGY (Amt. of energy necessary to break one mass of H2 into two masses of hydrogen atoms.) Example; Cl + Cl electron dot formula structural formula Cl-Cl empirical formula Cl2 1 mass Cl2 + 58 kcal yields 2 masses Cl atoms Ask what bond energy is. Example; 0 + O electron dot formula structural formula O=O empirical formula 02 Bond energy - 119 kcal/mole Example; N + N electron dot formula structural formula N=N empirical formula N2 Bond energy = 226 kcal/mole -Covalent bonds between unlike atoms H + Cl Name- hydrogen chloride or hydrochloric acid electron dot formula structural formula H-Cl empirical formula HCI one electron from each atom is shared with the other atom. 1 mass HCI + 103 kcal yields 1 mass H atoms + 1 mass Cl atoms Bond energy/ male as 103 kcal -Water molecules electron dot formula structural formula 49 empirical formula H20 1 mass H20 + 222 kcal yields 2 masses H atoms + 1 mass 0 atoms Ask the bond energy of 0-H Ask students to correctly combine in correct proportions: 1 N + H 1 C + H 1 C + Cl -Hydrogen Bands A weak chemical bond betwen a hydrogen atom in a molecule and a very electronegative atom in a second molecule. Electronegativity; The measure of a tendency of an atom in a molecule to attract shared electrons. O and N are highly electronegative when sharing electrons with H. (2 extra - charges) _ side electrons are drawn closer to 0 than H (2 protonsl+ charges) + side Discuss polar molecules H bonding when ice crystals form. -Disulfide Bonding certain situations -Reactions Combination A + X yields AX 50 Na + Cl yields NaCI Li + 02 yields Li02 Review electron exchange and ask Mg + 0 yields MgO which kind of bonds are formed (ionic) C + 02 yields 002 H2 + 0 yields H20 Review electron sharing and ask 0 + H4 yields CH4 what kind of bonds are formed (covalent) Decomposition AX yields A + X HgO + energy yields Hg + 0 (Let former chem students PbO + energy yields Pb + 0 know the equations are NaCl + energy yields Na + Cl not balanced, but we just want to see examples of decomposition reactions) Single Replacement reactions AX + B yields AB 4» X Cl + KBr yields KCI + Br Br + Kl yields KBr + l CI + Nal yields NaCl + I Double Re lacement reactions AX + BY yields AY + BX Al2(SO4)3 + Ca( H)2 yields AI(OH)3 + CaSO4 Explain how radicals sort of act like atoms. They have electrons to share. Bioenergetics Exergonic-any process which liberates energy as it proceeds. (show example) Endergonic-any process which absorbs energy as it proceeds. (show example) Biologically speaking-photosynthesis 6002 + 6H20 + sunlight yields C6H1206 + 6H20 Ask students whether it is exerganic or (endergonic). Why is sunlight necessary? 60 + 902 + 6H2 yields 6002 + 6H20 + energy 60 + 902 + 6H2 yields CeH1206 + 602 + less energy than above 51 don't write in . right away Therefore: CeH1206 + 602 yields 6002 + 6H20 (+ energy) Ask students, “How could we reverse the reaction? What would be necessary?” Have them diagram it going the other way. Make sure they include the energy involved. Ask where the energy comes from. Free Energy - F Change in Free Energy - delta F We now know that the absorption of light energy provides the necessary F to run the photosynthetic reactions. Give examples now and discuss F. A. Water flows downhill if given a chance to. Can the F In the water do work? How did the water get up high enough to flow downhill? B. Weights fall unimpeded. Can the F given off do work? How did the weights get high enough to fall? PULLEY AND WEIGHT DRAWING Which side of pulley gains F and which loses F? Same idea for chemical reactions. Acetyl Coenzyme A + 002 + 4.5 kcal/mole yields malonyl CoA Ask students, is F added to make it happen or is it given off when it happens? (added) Is this (endergonic) or exerganic Ask students, where does 4.5 kcal come from? answer, from an exerganic reaction -which is- ATP + H20 yields ADP + P + H ions + 8.9 kcal/mole Ask students, is F added to make it happen or given off? (given off) Is this reaction endergonic or (exerganic)? 52 Have students explain in their own written words how these two reactions are connected to one and other. If necessary go back to ionic and covalent bonding. Couplingce A tyl CoA + 002 + 4.5 kcal/mass yields malonyl CoA and (HP03) 8 ATP + H20 yields 8.9kcaI/mass + ADP + P + H+ These reactions are not connected to each other in any way. is. Draw pulley with one weight unattached. We must couple the 30# weight to the 25# weight by the rope. Similarly, we must couple reaction A from above to reaction B if the reaction is to occur. The rope is Acetyl caenzyme A carboxylase denoted as E. Biotin is a cofactor bound to E. E-biotin + 002 + ATP + H20 yields p E-biotinCOz + ADP + IIIPIOa + H + 4.2 kcaVM then E-biotin002 + AcetleoA yields E-biotin + malonleoA + 0.2 kcal/M The net result of these reactions is: AcetleoA + 002 + ATP + H20 yields Malonyl COA + ADP + HPOa + HI» «I 4.4 kcal/M Talk briefly about catalyst (enzyme) function in metabolisms. (DESCRIBE JOHN‘S DEMONSTRATION 0F CATALYSTS AND USE IT NEXT YEAR) pH and Buffers 53 LESSOV PLANS: CARBOHYDRATES - Functions; energy source for cells, carbon source, storage, cell structure - empirical formula (0H20)n -aldehydes or ketones that have two or more hydroxyl (OH) groups aldehyde if: ketone if: SIMPLE MONOSACCHARIDES -simplest monosaccharides with n=3 are trioses CaHaOa glyceraldehyde dihydroxyacetone Ask which is ketone and which is aldehyde. Because they are sugars we call them aIdOSE and ketOSE depending on the group present. Monosaccharides with 4,5,6,and 7 carbons (n) are called: tetroses, pentoses, hexoses, heptoses Two common hexoses: GLLKXBE FRUCTOSE Ask why they are monosaccharides. Ask which is an aldose and which is a ketose. Then ask why. (group recognition) I In solution these two hexoses are not open-chain structures. They cyclize and form rings. HAVE STUDENTS BUILD MODELS FROM KITS. THEN WORK THROUGH THE FORMATION OF THE RING STRUCTURE AS DRAWN BELOW. Because of the ring form the molecule will either be called a pyranose or furanose. This particular one is called (GLUCOPYRANOSE). Similarly the following is the formation of a furanose. This particular one is called (FRUCTOFURANOSE) -Horwath projections are diagrams of the previous but with the 0 for the carbon atoms of the rings left out. -Numbering of carbon atoms in hexoses glucose galactose fructose DISACCI-IARIDES -are formed by dehydration synthesis reaction. (diagram 1-4, 1-6 bonding) HAVE STUDENTS BUILD MODELS WITH KITS. TWO MONOSACCHARIDES FIRST. WHEN THEY COMBINE THE TWO DEFINE THE BONDS DESIRED. (1 -4, 16) -can be broken apart by hydrolytic reaction. sucrose a glucose + fructose lactose - glucose + galactose 55 maltose - glucose + glucose HAVE STUDENTS BREAK THE BONDS. (ASK WHERE ENERGY AND ATOMS COMES FROM) - sweetness of di and monosaccharides vary. Fructose very sweet. Lactose least sweet. -In humans, glucose is the most commonly transported sugar. ST ORAGEANDSTRUCTURALCARBOHYDRATES -called poly, and oligosaccharides -most carbo's are stored in living systems as polysaccharides of large mass. These are long chains (polymers) of monosaccharides. Glucose is the most common primary unit. to. starch, glycogen, cellulose, lignin -All three are composed of glucose units but have different properties due to linkage. HAVE STUDENTS BUILD DEFINED MONOSACCHARIDE. GET WITH PARTNER AND FORM A DISACCHARIDE. GET WITH ANOTHER GROUP AND FORM OIJGOSACCHARIDE. GET WTTH ANOTHER GROUP AND FORM POLYSACCHARIDE. WITH SMALL GROUPS HAVE THEM IDENTIFY THE 1-4, 1-6 BONDING POINTS. (ASK ABOUT THE LEFT- OVER WATER MOLECULES.) Starch- storage form in plants. Digestive tracts of animals secrete enzymes which can hydrolize starch into glucose units. These can then enter the bloodstream. Glycogen- main storage carbo of animal cells. (liver-blood/muscle-respiration) very large molecules sometimes 500,000 glucose units. Cellulose- major structural unit of plant cell walls. wood - 50% cotton - 98% largely unbranched chains which form hydrogen bonds between adjacent chains. (sometimes 100 - 200 chains together in a fiber. The many H bonds between make the chains resistant to dissolving in water. -The orientation of the glucose units determines which enzymes can fit into the bonded regions. Enzymes in animals can't fit into those points on cellulose or lignin, but can on starch and glycogen. -Some animals (rumenants-cattle, horses, sheep, deer) possess bacteria and protozoa in their digestive tracts. These organisms secrete enzymes which can break the bonds in the polysaccharide, and use the monosaccharides as food. As the microorganisms' populations increase they, and some of the monosaccharides, serve as nutrients for the animal. -Anecdote termite/cockroach eat cellulose, protozoans in their dig. tracts eat cellulose, bacteria in the protozoa digest the cellulose. chitin (exoskeleton of arthropods) is a structural polysaccharide. Difficult to hydrolize. Few animals possess the enzymes to do so. 56 PROTEINSLESSONPLANS: - Macromolecules (large) many functions Structural support, bone, cartilage, hair Enzyme catalysts, all enzymes are proteins, growth and cellfunctions Transport/storage, Transferrin/Fe, Hemoglobin/02, FerrItIn/stores Fe Movement, muscle fibers/actin and myosin Immunity, immunoglobulins Hormonal regulation, Thyroxine (released as thyroglobin), insulin Sensory perception, receptor proteins for light, neurotransmitters -The functional diversity is due to practically unlimited potential for structural variation. Composed of combinations of twen structurally different al ha amino acids. Amino Acids-an organic said w Ich possess an AMINO ROUP (NH3-) -and a CARBOXY L GROUP. (COOH') ~General structural formula: alpha carbon is the one to which the carboxyl group is attached. -lf the amino group is attached to the alpha carbon it is an ALPHA Amino Acid. HAVE STUDENTS FORM MODELS OF SIMPLE AMINO ACIDS. IMPRESS UPON THEM THAT THE STRUCTURAL DIFFERENCES BETWEEN AA’S IS THEIR R GROUP. HAVE THEM FORM GLYCINE AND ALANINE. Each amino acid Is identified by its side chain (R group). It is attached to the alpha carbon. . The size, shape, charge, H-bonding capacity, and chemical reactivity of an amino acid is mostly dependent upon its R-group. Side chains vary in complexity. glycine- 57 leucine- tryptophan- Have the students refer to the handout which describes the various R-groups and the polarity of the amino acids. ‘ -Variability of proteins: a small protein might contain 100 amino acids. 2100 combinations are possible in that case. sizes range from 50 to several hundred amino acids. complex organnisms have several thousand different kinds of proteins. arrangement of AA's gives each protein its own structural properties. The properties allow it to carry out its specific function. -Peptide Bond covalent bond between carboxyl group of one AA and the amino group of the neighboring AA. dehydration synthesis (Remind them that the band can therefore be broken by hydrolysis.) Dipeptide - 2 .AA's linked, Tripeptide - 3 AA's linked, etc. Handout diagrams of polypeptides. always a free amino group at one terminus and a free carboxyl at the other. free AA is the N-terminal, free carboxyl is the C-terminal. free N-terminal is considered the beginning of the molecule. when writing sequence, begin with this end. HAVE THEM WRITE THE SEQUENCE OF PART OF THE POLYPEPTIDE DIAGRAM. Three-D structure of proteins: (Use howard Hughes Foundation booklets) 4 levels-primary, secondary, tertiary, quaternary (USING THE RIBBED RIBBON ANALOGY DESCRIBE THE 4 LEVELS) primary-sequence of amino acids as determined by the DNA. secondary-alpha helix and beta pleated sheets due to bonding between AA's tertiary-bending and folding usually due to disulfide bonds and/or 58 hydrophobicity. quaternary-merism of the bended and folded molecules Breifly discuss sequence errors and how they might affect the shape and therefore function of a protein. Show N.I.H. movie on Sickle Cell Anemia (2 days) LIPIDS: -lnsoluble in water, soluble in organic solvents (i.e. acetone, benzene) demonstrate vegetable oil with water and with several solvents -Ihey are non-polar (water is polar - reinforce that like likes like) -three major categories: fats/oils ----------- storage compounds phosphoglycerides---- components of cell memb. steroids ----------- components of memb., vitamins, hormones Fats and Oils Fats- solid at room temp. and produced by animals. (lard, butter) Oils- liquid at room temp. and produced by plants. (corn, olive all) chemical group called esters - compounds formed by reaction between an alcohol and an acid. complete hydrolysis of one molecule of fat or oil yields glycerol, which is an alcohol, and from one to three long chain molecules called fatty acids. HAVE STUDENTS MAKE A GLYCEROL MODEL WITH KITS glycerol has three OH- groups so three fatty acids can be joined to it through the dehydration synthetic reaction. mono, di, tri acylglycerol depends on how many fatty acid molecules react with the glycerol molecule. HAVE STUDENTS MAKE MODELS OF MONOACYLGLYCEROL (H20 7) HAVE THE ACID GROUP BE 13 - 14 CS LONG. triacylglycerols accumulate in the fat cells. fatty acids - long zigzag chains of 0's, usually with two H's per 0, and always with a carboxyl (carboxylic acid) group 59 at one end of the chain. usually they are drawn as follows; butyric acid (main component of buttermilk.) HAVE STUDENTS MAKE A MODEL OF BUIYI’IC ACID. saturated/unsaturated fatty acids (double bonds) more than one set of double bonds - polyunsaturated ASK STUDENTS WHY THE WORD POLY IS USED. animal fats (solid) - saturated (no double bonds) plant oils (liquid) - unsaturated (double bonds) if plant oils are hydrogenated (break double bonds and add H's) they become solids. (i.e. margarine 8: peanut butter) we call these hydrogenated vegatable oils. HAVE STUDENTS MAKE MODELS OF STERIC ACID. GIVE THEM CNLY THE EMPIRICAL FORMULA. (C18H350H) HAVE STUDENTS MAKE MODELS OF OLEIC ACID. GIVE THEM ONLY THE EMPIRICAL FORMULA. (C18H330H) ASK STUDENTS WHERE OLEIC ACID MIGHT BE FOUND. (OLEO) ASK THEM WHICH OF THE ABOVE IS SATURATED. SHOW THEM WHERE THE DOUBLE BOND GOES. AND HAVE THEM CORRECT THEIR MODELS. - Lipids are a good energy source complete oxidation (burning) of fats/oils releases twice as much energy (calories/gram) as do carbohydrates and proteins. more water is produced when oxidized. (i.e. animals in hibernation/estivation need this water) animals (fat) store as much energy as plants (starch) in half the mass. ASK THE STUDENTS WHY THIS MAY BE BENEFICIAL TO THE ANIMAL'S SURVIVAL in mobile organisms (animals) less mass means more kilometers/ gram of fuel. (similarity to automobiles) 60 -Phasphoglycerides same as triacylglycerols except a phosphoric acid is substituted for a fatty acid, and an additional group is added to the phosphate. the additional group attached to the phosphate provides a region of strong polarity. oleic acid (018) saturated palmitic acid (016) unsaturated long chain portions are non-polar and therefore will not mix with water. ASK STUDENTS WHY. HINT: UKE LIKES ? additional group on phosphoglycerides is polar and will not mix with non-polar molecules. (THIS IS IMPORTANT WHEN DESCRIBING CELL MEMBRANE STRUCTURE, SO MAKE SURE THEY KNOW IT!) long chains of phosphoglyceride molecules don't like to be around water (BECAUSE ITS POLAR) and thus are said to be hydrophobic. USE THE TERM PHOBIA WITH HYDROPHOBIA AND CLAUSTROPHOBIA additional group portion of phosphoglyceride molecules like water (ASK WHY) and are attracted to it. They are called hydrophilic. polar region non-polar region ASK STUDENTS TO DIAGRAM THE ARRANGEMENT OF PHOSPHOUPID MOLECULES SITTING ON THE SURFACE OF WATER IN A BEAKER. 61 ASK STUDENTS TO DIAGRAM THE MOLECULAR ARRANGEMENT OF THE SPHERICAL BUBLES WHICH FORM WHEN OIL AND WATER ARE EMULSIFIED. (SUSPENSION/MICELLES) -Steroids four interconnected carbon rings (is. cholesterol, estradiol, testost.) HANDOUT DRAWINGS no relationship to fats/pile or phosphoglycerides. the reason they are classified as lipids is because they are soluble in organic solvents but not in water. (ASK STUDENTS IF THEY ARE POLAR 0R NON-POLAR) cholesterol is one of the most abundant, it Is found in the cellular membranes of all animals. i.e. it is a major component of Schwann cells which wrap around axons of nerve cells and act as insulators. it is a chemical precursor of important animal hormones (i.e. testosterone) a 132# human normally has 1/2# of chlosterol chlosterol tends to settle out of solution when present in high concentrations. sometimes precipitates from bile, forming W in the gall bladder. fatty / hardened accumulates in walls of arterioles (athero-scletosis) which contributes to; high blood pressure, stroke, and heart attacks EXPLAIN WHY IF TIME PERMITS APPENDIX F QUIZZES QUIZ #1 ' 1 N QUIZ #2 5. 62 DAILY QUIZZES The smallest piece of an element which retains the properties of the element is a(n) (ATOM) An _(I_QN)_ will have either more or less electrons than It does protons. . The four main energy levels are K, L, M, and N. What Is the maximum number of electrons one would expect to find In the L level? JIGHD— The symbol for the element potassium is ._.(.IS)_.. An atom which has an atomic number of 80 and an atomic mass of 200.59 Daltons will contain (121) neutrons. . Ionic compounds often W when placed in a solution of polar molecules. Ari atom which strongly attracts electrons is said to be a(n) was) agent. It energy must be provided to form an ion, the formed ion has what charge? _IEQSIIIME)_ An atom which has the atomic number 13 has its electrons in which main energy levels? ENEBGILEVEL NIMBEBQEELECIBQNS K ._.(2)_ L _(3)_ M _(3)_ N __(0)_ If an atom loses electrons we say it has been _I,QX1D_|ZEQ)_. QUIZ #3 63 USING YOUR PERIODIC CHART, ANSWER THE FOLLOWING QUESTIONS. 1. If energy is necessary for a reaction to occur, the reaction is said to 2. termed ___IENDEBGQNICJ__. How many electrons are there in the outside energy level of an atom with the atomic number of 15 ? (5) 3. Diagram an electron dot formula for an atom of magnesium. QUIZ #4 1. Diagram, with an electron dot formula, a molecule of carbon dioxide. Draw a structural formula for a molecule of carbon dioxide. Succinctly, and in your own words, explain Lambert's Law. [II I II I l I II' II . ll III'II nansminadJmmJa Briefly, and in your own words, explain Beer's Law. [II II' |||i II' Il'll III'III 'II II ill What can spectrophotometers be used for? ID | . . I' l . l I I . | l' | . W What is meant when we say we read transmittance from the Spec. 20? III | . II' IIII III“ 'II 30—I - l-:=I0I.III. 0. ‘0 now I: I-iz.“ .Iio: What is meant when we say we read absorbance from the Spec. 20? III I . l' H” In.“ .” I'l l H I'll I ,I N H . I molecules.) QUIZ #5 .5 . Using the beat juice graph, determine the wavelength of light which is least absorbed. _(610_nm)_ (close is good) 2. If we used paper chromatography on same boat juice, what should we see if our data is correct? WW 3. Using the boot juice graph, determine the wavelength at which the greatest amount of light was absorbed. Mum) 4. Using our data, and the fact that light at the wavelength of 680 nm seems to be transmitted most from the beet juice, we should see the color JBEDL when looking at the beef juice. 5. Using the graph of absorbance as a function of %T, interpolate the value of "Y" if the %T is 31. W (close ls good) QUIZ #6 LABEL EACH OF THE FOLLOWING CHEMICAL EQUATIONS AS TO TYPE. 1 . H20 + 80:; yields H2804 __.IC_QMBINAIIQN)__ 2. Ca + 2H20 yields Ca(OH)2 + H2 W 3. Cl2 + 2Nal yields 2NaCl + l2 W 4. H2804 yields H20 + 503 _ID.E9_QMEQS.IIIQN).__ 5. AB + CD yields AC + BD W 65 QUIZ #7 1. How many carbon atoms in a heptose? (7) 2. A carbohydrate must have more than two _I:IXD.BQXIL_ groups. 3. What is the correct general empirical formula for monosaccharides? ___ICI:lein_ 4. Which of the following is not a function of carbohydrates? a. W b. structural component of cells a. an energy source for cells d. a carbon source for cells 5. What Is the chemical structure which indicates an aldehyde? QUIZ #8 1. Which of the following does not belong to the group? a. lactose b. fiBUQIQSEL c. maltose d. sucrose 2. Which three letters at the end of a molecule's name idicate that the molecule is a protein? _(AS,E)_ 3. What affect can pH have on protein molecules? W 4. Which of the hexoses has a five-sided ring? __tEBu.QIQSEl_ 5. The process of breaking molecules apart by the addition of water is termed _II:IXDBQLYSISI__ QUIZ #9 1. List three functions of proteins. a. W OTHER POSSIBLE ANSWERS; D. W TRANSPORT/STORAGE, MOVEMENT, o. W IMMUNITY, STRUCTURAL/SUPPORT 2. __(E_QLYMEBS)_ of amino acids are called proteins. 3. The amino and carboxyl groups of amino acids are usually attached to the _IALEI:IA.CABBQN)_- 4. Diagram the structure of a carboxyl group. 66 5. The least complex residue of amino acids is I-HI QUIZ #10 1. The empirical formula NH2 represents a(n) _,(AM]NQ)_ group. 2. Diagram the structural formula of glycine. 3. Circle the carboxyl group. (only that group, no other atoms.) 4. Structurally diagram a dipeptide using the letter 'R" for residue. 5. Circle the carbon in the peptide bond. (Only the bond carbon) QUIZ #11 1. Enzymes are _(QAIALYSIS)_ because the influence the rate of reactions. 2. Which of the following will LL01 influence the rate of enzyme activity? a. the number of substrate molecules b. the number of enzyme molecules 0. CLHEEBESENCECEQIHEBENZMESI d. the pH of the environment 3. Metabolic paths can and do occur without enzymes but the process is __ISLQIIID__- 4. __(ANAB_QL|Q)_ metabolisms build larger structures. 5. Another name for a prosthetic group would be _(C_QEAC_‘LQB)__. QUIZ it 12 1. The major cellular function of phosphoglycerides is; ISIBUCIUBEOECELLMEMBBANESI. 2. A fatty acid with several double bonds is a(n)—(EQLYUNSAIUBAIEL fatty acid. 3. Glycerol is a three carbon _(ALC_QHQL)__. 4. Structurally diagram a diacylglycerol molecule. 5- Fatty acids are bonded to glycerol by a W reaction. 67 QUIZ #13 1. Gel electrophoresis separates molecules because of their _(Q|:|ABGE)__. 2. Mixtures between weak acid and salt of that acid are called _LB_LIEEEBS)_. 3. A solution with a pH of 5 would be represented by which of the following concentrations of H+, in moles/liter? a. .5 b.1x10 5th a. (.QQQQS), d. 5- 4. The negative of which of the following is the largest number? a.1x103rd b.(1_x__‘|_D_-_3,Ld), c.1x10 61h d. 1 x10 -2 5. The symbol representing the pH value when one half the buffer is dissociated is _(n|_<,)_. APPENDIX G TESTS 68 MOLECULAR BIOLOGY PRE/POST TEST HOLECULAR IIOLOEY FIRE-TEST FHOOSE THE BEST ANSWER (SO POINTS) I. SUBSTANCES WHICH DISSOCIATE IN POLAR SOLVENTS ARE. A. HYDROGEN BONDED . B. SULFIDE BONDED C. IONIC BONDED D. COVALENT BONDED 2. A SOLUTION WHICH HASA HYDROGEN ION CONCENTRATION OF( I X 10-?) PER LITER HASA pH OF, A. 7 B. IO C. -7 D. I 3. A SOLUTION WITH A pH OF ( I X I0-5) HYDROGEN IONS PER LITER WOULD BE CONSIDERED; A ACIDIC B. ALKALINE (BASIC) C. NEUTRAL 4. AN ATOM OF THE ELEMENT IRON HAS AN ATOMIC NUMBER OF 26 AND AN ATOMIC MASS 0F 0F 55.847 DALTONS. DETERMINE THE NUMBER OF NEUTRONS IN AN ATOM OF THIS SUBSTANCE. A. 26 B. 30 C. 56 D. 82 5. IF AN ATOM HASAN ATOMIC NUMBER OF I3, IT WILL HAVE HOW MANY ELECTRONS IN THE M ENERGY LEVEL? A. l3 8. 10 C. 8 D. 3 6. THE CHEMICAL SYMBOL FOR PHOSPHORUS IS; AP 8. Ph 0. Po D. Ps 7. IN THE EQUATION Mg + Br'z , WHICH ELEMENT HAS GAINED ELECTRONS? A. THE ONE WHICH HAS BEEN REDUCED. B. THE ONE WHICH HAS BEEN OXIDIZED C. THEY BOTH HAVE D. NEITHER HAVE 8. WHICH OF THE FOLLOWING IS EXERGONIC? + A. Na ATOMS + Il9 KCAL YIELDS I MOLE Na + I MOLEe . 8. CI ATOMS + ELECTRONS YIELDS I MOLE OF CI' + 83 KCAL. C. BOTH ONE AND TWO ARE EXERGONIC. D. NEITHER ONE NOR TWO ARE EXERNONIC. 9. 'THE EQUATION CI‘ * 2 Kl YIELDS 2 KCI + Ia. IS; A. COMBINATION B. DECOMPOSITION 0. SINGLE REPLACEMENT D. DOUBLE REPLACEMENT 10. AN ATOM WHICH HAS BEEN OXIDIZED WOULD BE CALLED A( N): A. CATION B. ANION C. POSITIVE D. NONE OF THESE THE NEXTTI'REE QUESTKNSNVOLVE THE FOLLOWS DATA RECORDED FROM SPECTROPHOTOMETRIC READNGS. THE FHSTRO‘W IS WAVELENGTHS, THE SECOND HOW IS PECBIT TRANSMSSION. 400 420 440 460 480 500 520 540 $60 580 600 620 640 .22 .22 .22 .25 .20 .28 .30 .35 .40 .52 .60 .75 .40 69 ii. The wavelength of Ilght most greatly absorbed is; a. 400 b. 480 c. 600 d. 640 12. The number of different colors our eyes would see when looking at the cuvette which gave the above readings would be: a. l b. 2 c. 3 d. 4 13. These/this colorts) would be: a. blue b. yellow and blue c. yellow d. green 14. Which of the following data supports Beer’s law? a. Twice the thickness of solution causes twice the absorbance. b. Twice the thlckness of solution causes half the absorbance. c. Twice the number of absorbing molecules causes twice the abs. d. Twice the number of absorbing molecules causes half the abs. is. Observation of precipitans are Important In the analytical technique called: a. gel permeation chromotograohy b. Ouchterlony diffusion c. spectrophotometry d. electrophoresis THE DATA IN THE FOLLOWING DIAGRAM OF AN ELECTROPHORETIC GEL SHOULD BE USED TO ANSWER THE NEXT THREE QUESTIONS. 4. (WEIIS) - I I III I I I l2l I I I I3I I I I 16. Which well 13; a. saturated b. unsaturated c. polyunsaturated Lipid molecules are: a. polar b. hydrophobic c. hydrophilic d. a and c Which of the following contain ring structures? a. neutral lipids b. phospholipids c. waxes d. steroids Which of the following is a carbohydrate? a. chitin b. glycerol c. vallne d. insulin Which of the following is a protein? a. chitin b. glycerol c. vallne d. insulin QUESTIONS 41-50 INVOLVE NAHING THE STRUCTURAL DIAGRAMS ON THE BOARD. 41. 45. 49. 42. 43. 44. 46. 47. 48. 50. 72 BIOLOGY ll TEST PROTEINS AND LIPIDS FILL IN THE BLANKS WITH THE BEST ANSWER. (20 POINTS) 1. 8. 10. 11. 12. 13. 14. 15. 16. 17. 18. That which makes one amino acid different from another is the The beginning of a polymer of amino acids is the termina. . The bonds which connect one amino acid to another would be called a bond. Bending and folding of polypeptides is due in part to bonding. Merism is the level of protein structure. The sequence of amino acids in a protein is primarily determined by Gel is a means of seperating protein by charge or mass. Proteins are formed on cell organelles called Hemoglobin serves the function of Daltons is the average mass of an amino acid. Higher than normal temperatures often cause proteins 0 . One of the amino acids containing sulfur is The R group, carboxyl group, and amino group are all attached to the carbon. Pgoteins treated with 808 would seperate in an electrical field y . The three types of lipids are; fats and oils, phospholipids, and Fats and oils are for the storage of form from acids and alcohols chemically combining. The alcohol found in diacylglycerol is 73 19. A fatty acid with a bend in the carbon chain is called 20. The lipid is important in the formation of testosterone. MULTIPLE CHOICE: (10 POINTS) 21. Which of the following is not an amino acid? A. alanine B. glycine C. adenine D. glutamic acid 22. Hemoglobin is a; A. monomer B. dimer C. trimer D. tetramer 23. Which of the following is not a fatty acid ? A. stearic acid B. oleic acid C. butyric acid D. glutamic acid 24. Diacylglycerol is partially soluble in polar as well as non-pola solvents and is said to be; A. amphipathio B. hydrophobic C. hydrophilic D. insoluble 25. Which of the followin is solid at room temperature? A. peanut oil B. sun ower oil C. corn oil D. hydrogenated olive oil 26. Which of the followin is not a function of proteins? A. carrier of materias in the molecular form. B. formation of particular cell structures. C. energy storage. D. regulation of hormonal functions. 27. Which of the following is not a secondary determiner of protein structure? A. beta pleated sheets. B. disulfide bonding C. alpha helix 28. Which of the following is the most common molecule in cell 1'91"”??? l B d' l I l . rlacygyceros . lacy yceros C. carrier proteins D. hospgiolipids 29. Equal amounts of which of t e followmg could generate the most energy? A. carbo ydrates B. proteins C. lipids 30. Which of the following regulates the production of the others? A. carbohydrates B. proteins C. lipids 31-40 Name each molecular structure drawn on the board. REFERENCES CITED 74 LITERATURE CITED BSCS green Version 1987 Kendall/Hunt Publishing Company, Iowa Bglbee, Rodger W. 8. Landes, Nance! M. " cience For Life and Livin - An lementary School Science Program-from Biological ciences Curriculum Study" Feb 90 Dickerson, Richard E. .8. Gels, Irving 1 969 Harper and Row, Publishers, NY Flannery. Maura "Biology Today -_- Communicating BioIOQY" Mar 88 NABT Frederic, Martini, Ph.D. 1989 Prentice Hall, New Jersey Gardner, Alan M. ”How-To-Do-It/Biotechnology in 3 Days" Oct 88 NABT 75 Ielsrud, Don 8. Leonard, William H. . " abs - What Research Says About Biology Laboratory Instruction” Ma 88 NA T Jacob, Stanley, W 8. Francone, Clarice A. El | IE I' . II 1982 W.B Saunders Company, Philapelphia Metcalfe, Williams 8. Castka 1986 Holt, Rinehart, NY Okebukola, P.A. ”Science Laboratory Behavior Strategies of Students Relative to Performance in and Attitude to Laboratory Work" 1985 Robertson, William C. ”Teaching Conceptual Understanding to Promote Students Ability to Do Transfer Problems" Newsletter March/April 1989 MSTA Rubin, Amram 8. Tamir, Pinchas ”Meaningful Learning in the School Laboratory" November/December 88 NABT Srere, Paul A. 8. Estabrook, Ronald, W. 1 978 Academic Press, NY 76 Suelter, Clarence H. 8. Hunter, Roberta "Coagulation Temperature of Chicken Egg White” Fall 87 Vander, Arthur J., Sherman, James H. 8. Lucian, Dorothy S. ll EI'I IIIII' IBIEI' 1 980 McGraw-Hill, NY 77 GENERAL REFERENCES Alberts, Bray, Lewis, Raff, Roberts, Watson 1983 Garland Publishing, Inc., NY Barrett, Abramoff, Kumaran, Millington 1986 Prentice Hall, New Jersey Bretscher, Mark S. ”The Molecules of the Cell Membrane" Oct 85 Doolitle, Russell F. ”Proteins" t 85 Downie, N..M.. 8. Heath, R.W. 1959 Harper 8. Bros., Publishers, NY Ferdinand, W. 1976 John Wiley 8. Sons, London Hagerman, Howard, H. Lectures on Statistical Analysis, un ublished NgsgéMSU Behavioral/Environmental orkshop Lehninger, Albert L. 1970 Worth Publishers, Inc., NY 78 Stryer, Lubert 1981 W.H. Freeman, San Francisco Weber, Klaus 8. Osborn, Mary ”The Molecules of the Cell Matrix” t 85 Weinber , Robert, A. ”The M9 ecules of Life" t 85 "IIIIIIIIIIIIIIIIIIIIIII