Chapter 2 quiz
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Chapter 2 quiz

Course Number: CHE 312, Spring 2008

College/University: SUNY Buffalo

Word Count: 1072

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Chapter 2 1. Which of the following is true regarding the chirality of amino acids found in proteins? a. Only L amino acids are found in proteins. b. Only D amino acids are found in proteins. c. Proteins contain both D and L amino acids. 2. Of the 20 amino acids from which proteins are made, which is most likely to be present with its R-group in a mixture of ionization states near physiological pH? a. Tyr b. His...

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2 1. Chapter Which of the following is true regarding the chirality of amino acids found in proteins? a. Only L amino acids are found in proteins. b. Only D amino acids are found in proteins. c. Proteins contain both D and L amino acids. 2. Of the 20 amino acids from which proteins are made, which is most likely to be present with its R-group in a mixture of ionization states near physiological pH? a. Tyr b. His c. Glu 3. The conversion of cysteine to cystine is what kind of reaction? a. an oxidation b. a reduction c. an addition 4. Which of the following is NOT true of peptide bonds? a. They tend to be planar. b. They are generally in the trans and rarely in the cis configuration c. They tend to have the amide nitrogen protonated to give a positive charge. 5. What do -helices and -sheets have in common? a. Both are stabilized by hydrogen bonding involving the same types of groups b. The same amino acids stabilize both forms of secondary structure. c. The length of a 10-amino acid -helix and -sheet strand will be the same 6. Water-soluble proteins such as myoglobin tend to a. fold such that hydrophobic amino acid R-groups are on the interior of the protein and hydrophilic groups are on the outside b. fold such that hydrophilic amino acid R-groups are on the interior of the protein and hydrophobic groups are on the outside c. fold such that all peptide bonds form hydrogen bonds with water 7. -helices and -sheets are often found to be amphipathic. This means that a. They have positive charges on one side and negative charges on the other. b. They have large R-groups on one side and small R-groups on the other as small groups are easier to pack in the interior of the protein. c. They have one side or face that is predominately polar with the other side being predominately hydrophobic. 8. The major conclusion of the experiment of C. Anfinsen involving ribonuclease was that a. The information on how the protein should fold was contained in the amino acid sequence. b. A denatured protein loses its enzymatic activity. c. The protein could be refolded correctly only if the disulfide bonds were left intact. 9. Protein folding is often described as a highly cooperative process. This means that a. The folding of a given protein requires cooperation of a number of other proteins b. The folding of a protein is largely an all-or-none process c. A protein only folds correctly when present in its normal cellular environment. 10. For the peptide, Ala-Arg-Lys-Ala-Asn-Ser-Ala-Ser, what would be the expected charges at pH 1, 7, and 13? a. +3, +3, 0 b. +2, +2, -1 c. +3, +2, -1 1. Which of the following is true regarding the chirality of amino acids found in proteins? a. Only L amino acids are found in proteins. b. Only D amino acids are found in proteins. c. Proteins contain both D and L amino acids. Correct. With the exception of glycine, which is achiral, all other amino acids in proteins are L amino acids. 2. Of the 20 amino acids from which proteins are made, which is most likely to be present with its R-group in a mixture of ionization states near physiological pH? a. Tyr b. His c. Glu Correct. Of the three choices, histidine is the only one with an R-group pKa whose (6.0) is close to physiological pH. 3. The conversion of cysteine to cystine is what kind of reaction? a. an oxidation b. a reduction Correct. The reaction requires the removal of two electrons and two protons. The loss of electrons makes it an oxidation. 4. Which of the following is NOT true of peptide bonds? a. They tend to be planar. b. They are generally in the trans and rarely in the cis configuration c. They tend to have the amide nitrogen protonated to give a positive charge. c. an addition Correct This statement is NOT true. Peptide bonds are amide linkages in which the nitrogen bears no charge . 5. What do -helices and -sheets have in common? a. Both are stabilized by hydrogen bonding involving the same types of groups b. The same amino acids stabilize both forms of secondary structure. c. The length of a 10-amino acid -helix and -sheet strand will be the same The -helix will be shorter as it is more like a coiled spring while the -sheet is like an extended chain. 6. Water-soluble proteins such as myoglobin tend to a. fold such that hydrophobic amino acid R-groups are on the interior of the protein and hydrophilic groups are on the outside b. fold such that hydrophilic amino acid R-groups are on the interior of the protein and hydrophobic groups are on the outside c. fold such that all peptide bonds form hydrogen bonds with water Correct. Having polar groups exposed to surface and able to interact with water and hydrophobic groups in interior away from water is energetically beneficial. 7. -helices and -sheets are often found to be amphipathic. This means that a. They have positive charges on one side and negative charges on the other. b. They have large R-groups on one side and small R-groups on the other as small groups are easier to pack in the interior of the protein. c. They have one side or face that is predominately polar with the other side being predominately hydrophobic. The amphipathic character has nothing to do with charge. 8. The major conclusion of the experiment of C. Anfinsen involving ribonuclease was that a. The information on how the protein should fold was contained in the amino acid sequence. b. A denatured protein loses its enzymatic activity. c. The protein could be refolded correctly only if the disulfide bonds were left intact. Correct. Full activity was observed upon removal of denaturant and mercaptoenthaol. Thus, the totally unfolded protein "knew" how to fold up correctly. 9. Protein folding is often described as a highly cooperative process. This means that a. The folding of a given protein requires cooperation of a number of other proteins b. The folding of a protein is largely an all-or-none process c. A protein only folds correctly when present in its normal cellular environment. Correct. Proteins tend to be folded or unfolded without the presence of partially folded states. 10. For the peptide, Ala-Arg-Lys-Ala-Asn-Ser-Ala-Ser, what would be the expected charges at pH 1, 7, and 13? a. +3, +3, 0 b. +2, +2, -1 c. +3, +2, -1 Correct. Four ionizable groups must be considered: the N-terminal amino group, the arginine R-group, the lysine R-group, and the C-terminal carboxyl group.

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