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CHAPTER 3

MACROMOLECULES

I. Functional groups in organic compounds A. attached to C atoms B. are most often involved in chemical reactions C. presence gives molecules unique properties D. amino acid as example Students responsible for 7 functional groups - be able to name, recognize and describe them. See fig. 3.1 II. Isomers A. compounds that have the same molecular formulas, but dif. structures, and therefore dif. properties. 2 types: 1. structural - differ in arrangement of atoms 2. optical mirror images of each other often called left and right ( L and D). Often only 1 or the other is biologically active III. Organic polymers A. when small organic molecules (monomers) are joined together huge macromolecules (polymers) are formed B. 4 classes: macromolecule (polymer) 1. carbohydrates 2. lipids 3. proteins 4. nucleic acids monomer monosaccharide fatty acids amino acids nucleotides

C. condensation reaction: 2 monomers are linked together by removing a water molecule D. hydrolysis reaction: a polymer is broken down into individual monomers by adding a water molecule fig. 3.4 E. special helper proteins, called enzymes, are needed for these reactions to take place. IV. PROTEINS - C,H,N,O,S A. most abundant macromolecule in the cell B. structural, transport, hormonal functions C. accelerate chemical reactions in cells in the form of enzymes D. proteins very diverse in living organisms, yet all proteins (polymer) composed of various amts. and proportions of same amino acids (monomer) 1. 20 dif. amino acids in all living things 2. amino acid structure: table 3.2 3. amino acids are linked together by a peptide bond (dehydration) a. N and C terminus b. partial charges E. Levels of protein structure: fig. 3.7 1. primary - arrangement of amino acids linked by peptide bonds a. ultimately determines final shape b. sequence of a.a.s determined by genes

2. secondary - helix, pleated sheet - due to hydrogen bonds 3. tertiary - resulting from various bonding between R groups - ionic, hydrophobic, van der Waals, and disulfide bridges. 4. quaternary - two or more peptide chains held together in one functional unit F. shape = function 1. denaturation 2. chaperonins V. Carbohydrates CH2O A. function in short-term energy, cellular structures B. monosaccharides 1. one monomer containing 3 - 7 Cs each 2. many are structural or geometric isomers of each other 3. pentoses 4. glucose, fructose, galactose (6 Cs) a. forms of glucose: C. disaccharides 1. condensation makes glycosidic linkage 2. glu + fru = sucrose (table sugar) 3. glu + gal = lactose 4. glu + glu = maltose

D. polysaccharides 1. huge polymer consisting of hundreds to 1000s of monosaccharides 2. monomer is usu. glucose 3. examples of polysaccharides: a. starch b. glycogen c. cellulose E. modified carbohydrates 1. glucosamine and galactosamine 2. chitin VI. Lipids A. consist of mainly C and H, a few O B. nonpolar (hydrophobic) C. types of lipids: 1. fats: glycerol + 3 fatty acids a. saturated - no double bonds b. unsaturated - double bonds 2. phospholipids a. polar and nonpolar regions b. major component of plasma membranes 3. carotenoids 4. steroids - ringed structure: 5. vitamins 6. waxes fig. 3.20

VII. Nucleic acids DNA, RNA C,H,N,O,P A. DNA 1. makes up chromosomes, genes 2. DNA is converted to RNA, which is then translated into a particular protein. 3. replicated prior to cell division 4. sequences compared to establish evolutionary relationships b/t organisms B. RNA 1. synthesized from DNA 2. specifies the a.a sequence in a protein 3. makes peptide bonds b/t a.a. in ribosomes ribozymes C. nucleic acids (polymer) made up of many nucleotides (monomer) 1. structure: fig. 3.24 a. pentose sugar ribose, deoxyribose b. nitrogenous base A, T, G, C, U c. phosphate group 2. linked together by pentose and phos. D. some nucleotides are not hooked together to make nucleic acids: 1. ATP - adenosine triphosphate fig. 6.5 2. NADH, NADPH fig. 7.4 VI. Lifes origins A. extraterrestrial 1. evidence B. chemical evolution

1. Miller-Urey experiment 2. refinements 3. polymerization of monomers


-----------------------------------------------------------------------------------------------------------------OBJECTIVES FOR CHAPTER 3 1. Define condensation and hydrolysis 2. Know the monomers that make up proteins, lipids, carbohydrates, and nucleic acids 3. Define and describe the three polysaccharides, and know what monomers are put together to build them. 4. Know the function of the various carbohydrates presented 5. Know the function of the various lipids presented 6. Distinguish between saturated and unsaturated fatty acids 7. Know the structure and function of phospholipids and steroids 8. Define enzyme 9. Describe the 4 levels of protein structure and what types of bonds are involved in each. 10. Define peptide bond, R group 11. Define denaturation and what causes it. Understand the relationship between protein shape and function. 12. Know what type of molecule ATP and NADH are, and their biological importance. 13. Give examples of nucleic acids and their functions 14. Know the types of atoms each of the macromolecules is made of 15. Describe hypotheses on the origin of macromolecules 16. Be able to name and recognize the 7 functional groups presented in this chapter, and if any of the 7 are acidic or basic. 17. Do Self-Quiz questions 1-6, 8-10

SAMPLE QUESTIONS FOR CHAPTER 3 1. The sequence of amino acids in a polypeptide chain determine a. primary structure of carbohydrates b. primary structure of proteins c. primary structure of ions d. isotope formation e. ionic formation 2. Proteins capable of speeding up specific chemical reactions are called a. enzymes b. peptides c. messengers d. ions e. compounds 3. Which of the following are major components of cell membranes? a. carbohydrates b. phospholipids c. nucleic acids d. fatty acids e. sterols 4. Most plant oils are a. liquid at room temperature b. unsaturated c. solid at room temperature d. saturated e. a and b only 5. Genetic material is made up of primarily a. proteins b. polysaccharides c. triglycerides d. lipids e. DNA 6. The cell walls of plants are composed of a. cellulose b. starch c. glycogen d. hemoglobin e. chitin

7. ATP is an example of a. a protein b. a carbohydrate c. a lipid d. a nucleic acid e. a nucleotide 8. When egg white, a protein, is heated, it changes its structure from liquid to solid. The protein is said to be _____________ by the heat. a. hydrolyzed b. denatured c. transmogrified d. disfunctionalized e. condensed 9. Which of the following atoms is NOT found in nucleic acids? a. C b. H c. N d. O e. S 10. The secondary structure of a protein a. could be an -helix b. could be a -pleated sheet c. is held together by hydrogen bonds d. is made up of amino acids e. all of the above 11. Carbon can form covalent bonds with how many other atoms? a. one d. four b. two e. five c. three

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