Assuming that a polypeptide chain has only one alpha-helical conformation and that there

are 3 possible
orientations for each amino acid residue in the random-coil state, calculate S for the
conformational change:
Alpha-helix a random coil
for a polypeptide of 100 residues. What value of H per residue would be required to make
the melting point be
50C? Compare this with the hydrogen-bond energy, estimated to be 0 to 12 kJ/mol.
Based on the curves, which is a more effective denaturant? Why? Also consider the
structures of each denaturant.
b) Estimate the G of unfolding using both denaturation curves, assuming a two-state
mechanism (use at least 5
points for each curve). Compare and discuss any differences or similarites in the G values
obtained. What do the
values imply about the extent of and mechanism of unfolding using each denaturant?
Cytochrome f operates as a redox agent in chloroplast photosynthesis. The standard
reduction potential, of
cytochrome f at pH 7.0 is determined by coupling it to an agent of known such as
ferricyanide|ferrocyanide. In a
typical experiment carried out spectrophotometrically, a solution at 25C and pH 7.0
containing a ratio [Fe(CN)64-] /
[Fe(CN)63-] equal to 2.0 is found to have a ratio [Cyt f(reduced)]/[Cyt f(oxidized)] at 0.10 at
equilibrium.
a. Calculate the reduction potential for Cyt f
b. On the basis of the standard reduction potential, , for the reduction of O 2 to H2O at pH 7
and 25C is
oxidized Cyt f a good enough oxidant to cause the formation of O2 from H2O at 25C and pH
7?