Chapter 6, Problem 7P

a. Based on a more conservative answer to Problem 6 (2.7 x 10⁹² conformations), estimate the conformational entropy change on folding a mole of this protein into a native structure with only one conformation. (Hint Consider Equation )
b. If the protein folds entirely into a helix with H bonds as the only source of enthalpy of stabilization, and each mole of H bonds contributes -5 kJ/mol to the enthalpy, estimate $\Delta$ H_folding . Note that the ends of helices contain fewer hydrogen bonds per residue than in the middle (see Figure 6.4).
c. From your answers (a) and (b), estimate $\Delta$ G_folding for this protem at 25^oC. Is the folded form of the protein stable at 25^oC?

6. Consider a small protein containing 101 amino acid residues. The protein backbone win have 200 bonds about which rotation can occur. Assume that three orientations are possible about each these bonds.
a. Based on these assumptions, about how many random-con conformations will be possible for this protein?
b. The estimate obtained in (a) is surety too large. Give one reason why.