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FINAL EXAM I. __________________/
December 19, 1998 Biochemistry I II. __________________/ 50 BI/CH421, BI601, BI/CH III. __________________/ 32
IV. __________________/ 73
TOTAL /
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.).
- 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 K a values as shown? (Assume that there is no direct interaction between the buffer molecule and the enzyme to be studied.) Acid K a
A. Phosphoric acid 7.3 x 10- B. Lactic acid 1.4 x 10- C. Acetic acid 1.2 x 10- D. Dihydrogen phosphate ion (H 2 PO 4 - ) 6.3 x 10- E. Bicarbonate ion (HCO 3 - ) 6.3 x 10-
- In the diagram below, the plane drawn behind the peptide bond indicates the:
H
C Ca N
H R
O
C a
A. plane of rotation around the Ca-N bond. B. absence of rotation around the C-N bond because of its partial double bond character. C. region of steric hindrance determined by the large C=O group. D. theoretical space between -180∞ and +180∞ that can be occupied by the j and f angles in the peptide bond. E. region of the peptide bond that contributes to a Ramachandran plot.
- Which of the following amino acids is the most soluble in water at pH 7.0?
A. Glutamate B. Tryptophan C. Leucine D. Tyrosine E. Phenylalanine
- The folded states of globular proteins in aqueous solutions are stabilized primarily by ______.
A. hydrophobic interactions B. peptide bonds C. phosphodiester bonds D. ionic bonds E. disulfide bonds
- Which of these statements about enzyme-catalyzed reactions that obey Michaelis-Menten kinetics is false?
A. At saturating levels of substrate, the rate of an enzyme-catalyzed reaction is proportional to the enzyme concentration. B. The Michaelis-Menten constant K m equals the [S] at which V = 1/ V max. C. If enough substrate is added, the normal V max of a reaction can be attained even in the presence of a competitive inhibitor. D. The rate of a reaction decreases steadily with time as substrate is depleted. E. 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. largest kcat B. largest K m C. largest kcat/ K m D. smallest kcat / K m E. smallest K m
- Certain restriction enzymes produce cohesive (sticky) ends. This means that they:
A. cut in regions of high GC content, leaving ends that can form more hydrogen bonds than ends of high AT content. B. make a staggered double-strand cut, leaving ends with a few nucleotides of single-stranded DNA protruding. C. cut both DNA strands at the same base pair. D. stick tightly to the ends of the DNA it has cut. E. have none of the above characteristics.
- The basis of precipitation of proteins by ammonium sulfate is best described by which of the following statements?
A. Proteins are rendered insoluble when they bind the ammonium ion. B. Proteins are rendered insoluble when they bind sulfate ion. C. Addition of ammonium sulfate adjusts the pH to the isolectric point of the proteins. D. Ammonium sulfate binds water molecules, making them less available for hydration of proteins. E. 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. 6. B. 6. C. 7. D. 7. E. 8.
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Two heme proteins, X and Y, each combine reversibly with oxygen. Based on the O 2 -binding properties shown in the graph above, which of the following statements about proteins X and Y best explains these results?
A. X is hemoglobin and Y is myoglobin. B. X combines with O 2 more rapidly than does Y. C. X has a higher affinity for O 2 than does Y. D. X molecules bind more O 2 than do Y molecules. E. X 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. Gly B. Arg C. His D. Asp E. Asn
- Which of the following lists represent bonding interactions in their general order of strength on a "per bond" basis from lowest to highest?
A. hydrogen, ionic, hydrophobic, covalent B. hydrogen, hydrophobic, ionic, covalent C. ionic, hydrophobic, hydrogen, covalent D. hydrophobic, hydrogen, ionic, covalent E. covalent, hydrophobic, hydrogen, ionic
- Which of the following molecules or substances contain, or are derived from, fatty acids?
A. glycerolphospholipids B. beeswax C. triacylglycerols D. sphingolipids E. All of the above are derived from fatty acids.
- Tay-Sachs disease is the result of a genetic defect in the metabolism of:
A. triacylglycerols. B. gangliosides. C. sterols. D. vitamin D.
- Which vitamin is derived from cholesterol?
A. A B. B 12 C. D D. K E. E
- Which of these statements about the composition of membranes is generally true?
A. The lipid composition of all membranes of eukaryotic cells is essentially the same. B. All biological membranes contain cholesterol. C. Free fatty acids are major components of all membranes. D. The inner and outer membranes of mitochondria have different protein compositions.
- Peripheral membrane proteins:
A. penetrate deeply into the lipid bilayer. B. can only be released from membranes by detergent treatment. C. behave like typical soluble proteins when released from membranes. D. 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. putting longer-chain fatty acids into its membranes. B. putting more unsaturated fatty acids into its membranes. C. increasing its metabolic rate to generate more heat. D. synthesizing thicker membranes to insulate the cell.
- In glycoproteins, the carbohydrate moiety is always attached through the amino acid residues:
A. tryptophan, aspartate, or cysteine. B. asparagine, serine, or threonine. C. glycine, alanine, or aspartate. D. aspartate or glutamate. E. glutamine or arginine.
- The structure of NAD+^ does not include:
A. an adenine nucleotide. B. riboflavin. C. a pyrophosphate bond. D. two ribose residues. E. the vitamin nicotinic acid.
- Which of the following molecules binds strongly to avidin?
A. pantothenic acid B. folic acid C. niacin D. lipoic acid E. biotin
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The double-reciprocal plot shown above depicts which of the following types of enzyme inhibition by I?
A. uncompetitive B. competitive C. noncompetitive D. suicide E. 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.
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- (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 Answer Sheet 12/19/ Test Correct Question Answer
Multiple Choice 1 B 2 B 3 A 4 A 5 E 6 C 7 B 8 C 9 A 10 D 11 E 12 D 13 B 14 C 15 D 16 D 17 E 18 B 19 C 20 D 21 C 22 B 23 D 24 C 25 A 26 C 27 B 28 A 29 B 30 B 31 E 32 B STRUCTURES
- A. Deoxyguanosine B. part of nucleic acids
- A. Biocytin B. carbon dioxide carrier C. biotin is part
- A. NADH B. electron (hydride) transfer C. niacin is part
- A. Coenzyme A B. acetate or acyl carrier C. pantothenic acid is part
- A. Steric acid
- A. Linoleic acid
- A. Sphigosine
- A. Phosphatidyl choline (1-palmityl, 2-olyl) B. part of membranes
- 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
