Fill in the blanks. hydrophobic
Δ G unfolding (wt)
Destabalizing
ΔH
a big issue
Δ S protein
destabalize
different
hydrophilic
stabalize
Δ G unfolding mutant
Δ S protein
not an issue
destabalization
stabalization
stabilizing
similar
Δ S solvent
Because the mutation is on the surface, loss of contacts in the protein core is and the amino acid is likely to be interacting with solvent to extents in both folded and unfolded states; thus, effectsare predicted to be minimal.
The is likely to be small because side-chain solvation is predicted to be a big issue in both the folded and unfolded states. Achanges the most due to the conformational flexibility of Gly compared to Pro. Gly will both the folded and the unfolded states, however, it will the unfolded state more due to the dramatic increase in conformational stabilize entropy of the unfolded state as a result of this mutation.
The of the unfolded state for the mutant means that is greater than ; thus, the mutation is .