Chapter 8, Problem 4P

The folding and unfolding rate constants for a myoglobin mutant have been determined. The unfolding rate constant ${\text{k}}_{\text{F}}{{}_{\to }}_{\text{U}}$ = 3.62×10-5 S-1 and the folding rate constant ${\text{k}}_{\text{F}}{{}_{\to }}_{\text{U}}$ = 255 S-1, where F is the folded protein and U is the unfolded (denatured) protein. For wild-type myoglobin, ${\text{ΔG}}^{\text{'}}{}_{\text{F}\to \text{U}}$ = +37.4 kJ/mol. Which myoglobin is more thermodynamically stable, the mutant or the wild-type?