The folding and unfolding rate constants for a myoglobin mutant have been determined. The unfolding rate constant kF → U = 3.62 × 10−5s−1 and the folding rate constant kU → F = 255 s−1, where F is the folded protein and U is the unfolded (denatured) protein. For wild-type myoglobin, ΔG°′F → U = +37.4 kJ/mol. Which myoglobin is more thermodynamically stable, the mutant or the wild-type?
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