Homework3 - 4 What is the primary driving force causing a...

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BMB 461 Fall Semester 2008 Homework Assignment #3 Key posted Tuesday, September 16 This problem set covers material presented in Chapters 4 and 5. In addition to the questions below, you should look at the following questions in your textbook: Chapter 4 (pp. 149-150), nos. 1, 3, and 5, and Chapter 5 (pp. 180), nos. 1, 2, and 5. Solutions are in the back of the book. 1.) Why are the α -carbons and R groups of amino acid peptide linkages typically found in trans rather than cis conformation? What is the only amino acid commonly found in the cis conformation? Why? 2.) (a) What are the general distinctions between fibrous and globular proteins? (b) For each of α -keratin, collagen, and silk fibroin, what is the fundamental secondary structure that makes up the protein? How are the individual pieces of secondary structure assembled into larger structures? 3.) Explain how a deficiency of vitamin C causes the observed symptoms of scurvy.
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Unformatted text preview: 4.) What is the primary driving force causing a protein’s folded structure to be more stable than the unfolded state? How does this create a minimum size for a stably folded protein or protein domain? 5.) Describe the Anfinsen experiment and the main conclusion derived from it. 6.) What are the possible roles of protein disulfide isomerase and the chaperonins in protein folding in vivo ? 7.) What does the parameter θ represent in the case of myoglobin? What about hemoglobin? 8.) What is the significance of the observation that the Hill parameter for hemoglobin, ca. 3, differs from the number of oxygen binding sites (4) on a hemoglobin molecule? Under what conditions would a Hill parameter of 4.0 be observed? Under what conditions would a Hill parameter of 1.0 be observed?...
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This note was uploaded on 09/15/2008 for the course BMB 461 taught by Professor Stoltzfus during the Spring '07 term at Michigan State University.

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