Chemistry Final Exam Answer Key

NAME ________________________________ FINAL EXAM I. MULTIPLE CHOICE (245 points) Choose the BEST answer to the question by circling the appropriate letter. Questions 1-17 are worth 10 points each (170 pts.) and questions 18-32 are worth 5 points each (75 pts.). 1. An enzyme reaction to be studied at pH 4.0 can best be carried out using a buffer solution made from which of the following acids, and their conjugate bases, with Ka values as shown? (Assume that there is no direct interaction between the buffer molecule and the enzyme to be studied.) Acid Ka A. B. C. Phosphoric acid Lactic acid Acetic acid 7.3 x 10-3 1.4 x 10-4 1.2 x 10-5 D. Dihydrogen phosphate ion (H2PO4-) Bicarbonate ion (HCO3-) 6.3 x 10-8 E. 2. 6.3 x 10-11 In the diagram below, the plane drawn behind the peptide bond indicates the: O H C Ca N R Ca H A. B. C. D. E. plane of rotation around the Ca-N bond. absence of rotation around the C-N bond because of its partial double bond character. region of steric hindrance determined by the large C=O group. theoretical space between -180° and +180° that can be occupied by the j and f angles in the peptide bond. region of the peptide bond that contributes to a Ramachandran plot. 3. Which of the following amino acids is the most soluble in water at pH 7.0? A. B. C. D. E. 4. The folded states of globular proteins in aqueous solutions are stabilized primarily by ______. A. B. C. D. E. 5. Glutamate Tryptophan Leucine Tyrosine Phenylalanine hydrophobic interactions peptide bonds phosphodiester bonds ionic bonds disulfide bonds Which of these statements about enzyme-catalyzed reactions that obey Michaelis-Menten kinetics is false? A. B. At saturating levels of substrate, the rate of an enzyme-catalyzed reaction is proportional to the enzyme concentration. The Michaelis-Menten constant Km equals the [S] at which V = 1/2 Vmax. C. D. E. 6. attained even in the presence of a competitive inhibitor. The rate of a reaction decreases steadily with time as substrate is depleted. The activation energy for the catalyzed reaction is the same as for the uncatalyzed reaction, but the equilibrium constant is more favorable in the enzyme-catalyzed reaction. The most efficient substrate of an enzyme is usually considered to be the substrate with the ________. A. B. C. D. E. 7. If enough substrate is added, the normal Vmax of a reaction can be largest kcat largest Km largest kcat/Km smallest kcat/Km smallest Km Certain restriction enzymes produce cohesive (sticky) ends. that they: A. B. C. D. E. This means cut in regions of high GC content, leaving ends that can form more hydrogen bonds than ends of high AT content. make a staggered double-strand cut, leaving ends with a few nucleotides of single-stranded DNA protruding. cut both DNA strands at the same base pair. stick tightly to the ends of the DNA it has cut. have none of the above characteristics. 8. Two oligo-deoxynucleotides, 5'-ACCACGTAACGGA-3' and 5'-GTTAC-3', plus DNA polymerase are added to a reaction mixture containing the appropriate buffer plus radiolabelled dATP, dTTP, dCTP, and dGTP. The radiolabelled bases incorporated into the product of such a reaction would have which of the following base compositions? A. B. C. D. E. 9. A = 27% G = 30% T = 21% C = 22% If the genome of a newly isolated virus displays the base composition above, the virus most likely consists of ______. A. B. C. D. E. 10. single-stranded DNA double-stranded DNA single-stranded RNA double-stranded RNA a double-stranded RNA:DNA heteroduplex For protein synthesis, an amino acid needs to be attached by its ______ group to the _____ of the tRNA molecule. A. B. C. D. E. 11. 3C:2A 1G:1T 3G:2T 3G:3T:2C 5T:4G:3C:1A amino; phosphoryl group on the 5'-end carboxyl; phosphoryl group on the 3'-end carboxyl; hydroxyl group on the 5'-end carboxyl; hydroxyl group on the 3'-end amino; base on the 5'end The thymidine analog 3'-azidothymidine (AZT) blocks replication of human immunodeficiency virus (HIV). AZT is converted in cells to the 5'-triphosphate nucleotide derivative and then incorporatioed into cDNA copies of the infecting HIV RNA by the HIV's own reverse transcriptase. The cDNA terminates prematurely at the point of the inserted analog. The most likely reason that AZT is not equally inhibitory toward replication of human DNA is that the 5'-triphosphate nucleotide derivative is ___________. A. B. C. D. E. capable of base-pairing with the riboadenosine in the HIV RNA, but not with the deoxyadenosine in the human DNA replace with the normal deoxynucleotide during DNA replication unable to enter the nucleus, where DNA is replicated hydrolyzed by nuclear enzymes to the thymidine-5'-triphosphate, so the azido-form is not incorporated into replicating DNA bound with much lower affinity (resulting from a higher Km) to human DNA polymerase than to HIV reverse transcriptase. 12. The basis of precipitation of proteins by ammonium sulfate is best described by which of the following statements? A. B. C. D. E. 13. Proteins are rendered insoluble when they bind the ammonium ion. Proteins are rendered insoluble when they bind sulfate ion. Addition of ammonium sulfate adjusts the pH to the isolectric point of the proteins. Ammonium sulfate binds water molecules, making them less available for hydration of proteins. Ammonium sulfate amidates carboxyl groups on the proteins, rendering the proteins insoluble. The pH of a 10-8 M HCl solution prepared with pure water at pH 7.0 is closest to ____. A. B. C. D. E. 6.0 6.9 7.1 7.9 8.0 14. FIGURE DID NOT SCAN IN Two heme proteins, X and Y, each combine reversibly with oxygen. Based on the O2-binding properties shown in the graph above, which of the following statements about proteins X and Y best explains these results? A. B. C. D. E. 15. X X X X X is hemoglobin and Y is myoglobin. combines with O2 more rapidly than does Y. has a higher affinity for O2 than does Y. molecules bind more O2 than do Y molecules. is cooperative, but Y is noncooperative Proteins can be stabilized by bonds that could include the interaction of the side chain of a lysine residue with the side chain of ________. A. B. C. D. E. Gly Arg His Asp Asn 16. Which of the following lists represent bonding interactions in their general order of strength on a "per bond" basis from lowest to highest? A. B. C. D. E. 17. Which of the following molecules or substances contain, or are derived from, fatty acids? A. B. C. D. E. 18. B. C. D. B. B12 C. D D. K E. E The lipid composition of all membranes of eukaryotic cells is essentially the same. All biological membranes contain cholesterol. Free fatty acids are major components of all membranes. The inner and outer membranes of mitochondria have different protein compositions. Peripheral membrane proteins: A. B. C. D. 22. A Which of these statements about the composition of membranes is generally true? A. 21. triacylglycerols. gangliosides. sterols. vitamin D. Which vitamin is derived from cholesterol? A. 20. glycerolphospholipids beeswax triacylglycerols sphingolipids All of the above are derived from fatty acids. Tay-Sachs disease is the result of a genetic defect in the metabolism of: A. B. C. D. 19. hydrogen, ionic, hydrophobic, covalent hydrogen, hydrophobic, ionic, covalent ionic, hydrophobic, hydrogen, covalent hydrophobic, hydrogen, ionic, covalent covalent, hydrophobic, hydrogen, ionic penetrate deeply into the lipid bilayer. can only be released from membranes by detergent treatment. behave like typical soluble proteins when released from membranes. are generally bound covalently to phospholipid head groups. When a bacterium such as E. coli is shifted from a warm growth temperature to a cooler growth temperature, it compensates by: A. B. C. D. putting longer-chain fatty acids into its membranes. putting more unsaturated fatty acids into its membranes. increasing its metabolic rate to generate more heat. synthesizing thicker membranes to insulate the cell. 23. An integral membrane protein will commonly be solubilized by extraction with: A. B. C. D. E. 24. Which of the following monosaccharides is not an aldose? A. B. C. D. E. 25. and and and and and D-mannose D-maltose a-cellobiose L-fructose L-glucose D-glucose and L-glucose D-glucose and D-fructose a-D-glucose and b-D-glucose a-D-glucose and b-L-glucose D-glucose and L-fructose When the linear form of glucose cyclizes, the product is a(n): A. B. C. D. E. 28. D-glucose D-lactose a-maltose L-mannose D-glucose Which of following is an anomeric pair? A. B. C. D. E. 27. ribose glucose fructose glyceraldehyde erythrose Which of the following is an epimeric pair? A. B. C. D. E. 26. a buffer of alkaline or acid pH. a solution of high ionic strength. a chelating agent that removes divalent cations. a solution containing detergent. hot water. glycoside. hemiacetal. anhydride. lactone. oligosaccharide. Starch and glycogen are both polymers of: A. B. C. D. E. a-D-glucose. b-D-glucose. glucose-1-phosphate. sucrose. fructose. 29. In glycoproteins, the carbohydrate moiety is always attached through the amino acid residues: A. B. C. D. E. 30. The structure of NAD+ does not include: A. B. C. D. E. 31. tryptophan, aspartate, or cysteine. asparagine, serine, or threonine. glycine, alanine, or aspartate. aspartate or glutamate. glutamine or arginine. an adenine nucleotide. riboflavin. a pyrophosphate bond. two ribose residues. the vitamin nicotinic acid. Which of the following molecules binds strongly to avidin? A. B. C. D. E. pantothenic acid folic acid niacin lipoic acid biotin 32. FIGURE DID NOTT SCAN IN The double-reciprocal plot shown above depicts which of the following types of enzyme inhibition by I? A. B. C. D. E. uncompetitive competitive noncompetitive suicide covalent II. STRUCTURES: IDENTIFICATION & FUNCTION. (50 points) A. Identify the following structures by name (common, or trivial names preferred; systematic names OK, NO abbreviations) B. IF there is a blank for B., list one biologically significant function for that compound. Be as specific as possible. C. IF the compound shown is comprised of an essential vitamin, circle the vitamin part of the molecule. 1. THIS PAGE DID NOT SCAN IN: SEE KEY OUTSIDE DR. TOLAN'S OFFICE III. MATCHING. (32 points) Enter the appropriate letter in each blank. 34. All items will be used once. Match these molecules to their biological roles. __ __ __ __ __ 1. 2. 3. 4. 5. __ __ __ 6. 7. 8. carbohydrate storage in animal liver extracellular matrix of animal tissues blood clotting factor carbohydrate storage in plants polyanionic acid-sugar that forms core of proteoglycans structural component of plant cell walls disaccharide exoskeleton of insects A. B. C. D. E. proteoglycan starch chitin cellulose glycogen F. G. H. hyaluronic acid sucrose heparin IV. SHORT ANSWER. (73 points) Give a brief answer or diagram to each problem or question. 35. In the last structure shown on page 8, what products would you expect after exhaustive methylation and hydrolysis (just list the names)? What products would you expect following reaction with an a-glycosidase? (10 pts) 36. Write the inorganic reactants cell. (10 37. Describe the differences between a proteoglycan and a glycoprotein. (10 pts) complete reaction for the hydrolysis of ATP to ADP and phosphate. Briefly name three chemical differeneces between and products that explain the high DG for the reaction in the pts) 38. (43 pts) You have isolated the lysine aminoacyl tRNA synthetase and determined its structure. You are about to look for the most likely active site in your structure. A). Draw the structure of the intermediate that would be bound at the active site prior to transfer of the lysine to an incoming tRNALys. B). Surround this structure with a wavy line to indicate the surface of the enzyme active site. Show (and name) as many intermolecular interactions between the enzyme and the substrate intermediate you have drawn in (A). In each of the interactions you show suggest an amino acid residue that would provide a chemical group for such an interaction. These amino acids might be those for which you would look in your enzyme structure. C). Denote which residue in your enzyme that you might change by site-directed mutagenesis to investigate the fidelity of this enzyme. Which kinetic constant would you expect to change if you made such a mutant enzyme? D). Denote which residue in your enzyme that you might change by site-directed mutagenesis to investigate the activity of this enzyme. Which kinetic constant would you expect to change if you made such a mutant enzyme? FINAL EXAM Test Question Multiple Choice 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 STRUCTURES Answer Sheet Correct Answer B B A A E C B C A D E D B C D D E B C D C B D C A C B A B B E B 1. A. 2. A. Deoxyguanosine Biocytin 3. A. NADH 4. A. Coenzyme A 5. 6. 7. 8. part of nucleic acids carbon dioxide carrier biotin is part electron (hydride) transfer niacin is part acetate or acyl carrier pantothenic acid is part Steric acid Linoleic acid Sphigosine Phosphatidyl choline (1-palmityl, 2-olyl) B. part of membranes 9. A. Cholesterol B. part of membranes in animals, steroid or vitamin D precursor 10 A. Two Gal(a1,4)GlcNAc attached (b1,6) and (b1,2) to Man. C. Mannose is the reducing end. Matching A. A. A. A. B. B. C. B. C. B. C. Test Correct Question Answer MATCHING 34 Short Answer 35 36 E, A, H, B, F, D, G, C The structure is a sugar unit recognized by phytohemagglutinin: Two Gal(a1,4)GlcNAc attached (b1,6) and (b1,2) to Man. Products of methylation would be: 2,3,4,6 tetramethyl Gal, 3,6 dimethyl 2-N-acetyl Glc, 1,3,4 trimethyl Man. There would be Gal released by an a-glycosidase because of the (a1,4) links at the non-reducing ends. No glycolytic celavage after that because there are only b-linked sugars. ATP-4 + H2O <=====> ADP-3 + H2PO4-2 + H+ 1. Increase in resonance forms in the inorganic phosphate product. 2. Relief of charge repulsion between a and b phosphate groups on reactant, ATP-4 3. Deprotonation of the immediate product, ADP-2, to ADP-3 + H+. Thus pulling the equilibrium to the right. 37 38 Both are made up of proteins and polysaccharides. In proteoglycans, the carbohydrate moiety dominates, constituting 95% or more of the mass of the complex. In glycoproteins, the protein constitutes a larger fraction, generally 50% or more of the total mass. A. The structure should include AMP-amino acid (Adenine-ribose-phosphate-carboxyl linked lysine) intermediate. B. At a minimum there should be ionic interactions with the Lys, a-amino group, phosphate group provided by opposite charges coming from Glu/Asp/His/Arg/Lys; hydrogen bonds to the ribose and /or adenine base and amino acid carbonyl oxygen and the phosphate group (H-bonds whould show proper donor/acceptor orientation); hydrophobic interactions of the adenine and the methylene chain of Lys provided by amino acids such as Ala/Val/Ile/Leu/Met/Phe/Tyr, etc. C. This should denote the interaction with the Lysine e-amino group that affects Km. The change would be to Asp/Glu or neutral amino acid. D. This should denote changes in those amino acids in contact with the carbonyl oxygen and/or the phosphate group that affects kcat (or Vmax).