Q1)Molecular chaperones bind to unfolded or partially folded polypeptide chains
ID: 141465 • Letter: Q
Question
Q1)Molecular chaperones bind to unfolded or partially folded polypeptide chains in order to accomplish which of the following?
A: Facilitate aggregation of multiple subunits of a protein during synthesis.
B: All of the above are accomplished by molecular chaperones.
C: Facilitate native folding by exposing hydrophobic segments of the protein as it is synthesized.
D: Ensure that improper aggregation of hydrophobic segments does not occur.
E: Engulf the protein in order to ensure that the protein is not damaged by heat denaturation.
Q2)A helix has hydrogen bonds between the carbonyl group from residue “n” and the amino group of residue “n+6,” which of the following is TRUE?
A: It is an helix.
B: It has 3.6 residues per turn.
C: It is a random coil, not a helix.
D: It has fewer residues per turn than an helix.
E: It has more residues per turn than an helix.
Q3)Examine the three sequences below for collagen-like proteins. If hydrogen bonding were the most important feature in determining strength in fibrous proteins, which of the following sequences likely has the highest melting temperature and why? (Note: Flp = fluoroproline; Hyp = hydroxyproline)
A: “1” because the electronegativity of oxygen is greater.
B: “2” because the electronegativity of proline is greater.
C: “1” because Hyp has OH groups.
D: “3” because Thr is a small amino acid which allows close packing.
E: “2” because the electronegativity of the –OH group increases hydrogen bond strength.
1. Pro-Hyp-Gly-Pro-Hyp-Gly-Pro-Hyp-Gly 2. Pro-Flp-Gly-Pro-Flp-Gly-Pro-Flp-Gly 3. Gly-Pro-Thr-Gly-Pro-Thr-Gly-Pro-ThrExplanation / Answer
Q1. D
Molecular chaperones are basically protiens and the main function is to prevent Polypetide chains and subunits from aggregarion of nonfunctional oligomeric structures. The probablity of aggregation increases when protiens become denatured by stress. Chaperone block folding of protein by inhibiting steric information (Shape & Reactivity).
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