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.
- Spring '07