Fall2001Exam1withkey - Chemistry 695C Fall 2001 Exam 1 Key...

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Chemistry 695C Fall 2001 Exam 1 Key Multiple Choice 1. In an α -helix, the R groups on the amino acid residues: a) are found on the outside of the helix spiral. b) generate the hydrogen bonds that form the helix. c) stack within the interior of the helix. d) cause only right-handed helices to form. e) alternate between the outside and the inside of the helix. 2. Kendrew&s studies of myoglobin structure demonstrated that: a) the α helix predicted by Pauling and Corey was not found in myoglobin; β -pleated sheet structure was found. b) ±corners² between α -helical regions invariably contained a glycine residue, which, because of its unique properties, cannot fit into the helix. c) highly polar or charged amino acid residues tended to be located at the interior of the protein d) the structure was very compact, with virtually no internal space available for water molecules. e) the structure of myoglobin proved to be completely different from that of hemoglobin, as expected from their very different biological roles. 3. Experiments on denaturation and renaturation after the reduction and reoxidation of the ³S-S- bonds in the enzyme ribonuclease (RNase) have shown that: a) the primary sequence of RNase is sufficient to determine the formation of a specific secondary and tertiary structure. b) the enzyme, dissolved in water, is thermodynamically stable relative to the mixture of amino acids whose residues are contained in RNase. c) native ribonuclease does not have a unique secondary and tertiary structure. d) the completely unfolded enzyme, with all ³S-S- bonds broken, is still enzymatically active. e) the folding of denatured RNase into the native, active conformation, requires the input of energy in the form of heat. 4. A sequence of amino acids in a certain protein is found to be ³Ser-Gly-Pro-Gly-. The sequence is most probably part of a(n): a) β turn b) parallel β sheet c) α helix d) α sheet e) antiparallel β sheet 5. Protein S will fold into its native conformation only when protein Q is also present in solution. However, protein Q can fold into its native conformation without protein S. Protein Q, therefore, may function as a ____________ for protein S.
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a) molecular chaperone b) protein precursor c) ligand d) supersecondary structural unit e) structural motif 6. In the binding of oxygen to myoglobin, the relationship between the concentration of oxygen and the fraction of binding sites occupied can best be described as: a) hyperbolic b) sigmoidal c) linear with a positive slope d) linear with a negative slope e) random 7. An allosteric interaction between a ligand and a protein is one in which: a) two different ligands can bind to the same binding site. b) the binding of the ligand to the protein is covalent.
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Fall2001Exam1withkey - Chemistry 695C Fall 2001 Exam 1 Key...

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