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. Author manuscript; available in PMC: 2009 Aug 20.
Published in final edited form as: Chem Rev. 2006 Aug;106(8):3443–3467. doi: 10.1021/cr050317n

Figure 7.

Figure 7

Free energy changes associated with binding (−RT ln KD) and catalytic turnover (−RT ln kcat/ν) for a wild-type enzyme (wt) and a mutant form (mut). The difference free energy for binding of the mutant relative to the wild-type in the ground state (ΔΔGmut) and the transition state are shown (ΔΔG). An identical diagram can be drawn for chemical substitution of an oxygen for sulfur or a methyl group. See text.