However these bundles can also be used to bring two

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However, these bundles can also be used to bring two protein monomers together as a homodimer. That is, two solvent-exposed helices on each monomer combine to form the four-helix bundle. Based on what you know about these bundles, what types of residues (charged/nonpolar/polar) would you expect to be most important at driving this dimerization? Please support your answer in one or two brief sentences. (7 pts) 2) a. Although enthalpy and entropy oppose each other in protein folding, the protein does manage to fold. Therefore, which is the dominant force in folding? (3 pts) b. In protein folding, which is the driving force in forming the molten globule? (3 pts) c. Both the unfolded and folded states contain many hydrogen bonds. As a result, hydrogen bonding is not a major net contributor to the free energy that drives protein folding. How do the hydrogen bond pairs in the unfolded and folded states differ? (5 pts)
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BIBC 100 Name: ___________________ Winter 2011 Midterm/Montal 4 [N-end] KRKIAVPTSCNQPPGPKRRKAMVYNQVSDDE [C-end] 3) a. How many hydrophobic amino acids are in the above sequence? Exclude glycine when counting. Draw two amino acids from the above sequence and write their full names. (5 pts) b. Will the above sequence in its entirety form a stable α - helix? Explain. (5 pts)
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BIBC 100 Name: _______________________ Winter 2011 Midterm/Montal 5 4) What motif is depicted in Figure A? Give one example of a protein that contains this motif. Where is the coordination site? (5 pts) What is the motif of Figure B? Give one example of a protein that contains this motif. (3 pts) What is the motif of Figure C? Name two topological arrangements possible for this motif. (3 pts) a. c. b.
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BIBC 100 Name: ___________________ Winter 2011 Midterm/Montal 6 5) a. Myoglobin and hemoglobin are examples of what type of α -domain structure?
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