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. 2008 Sep 4;105(37):13865–13870. doi: 10.1073/pnas.0804512105

Fig. 2.

Fig. 2.

Free energy profiles of HγD-Crys. (A) Free energy surface, F(x, y) for the wild type. (B) F(x, y) for the circular permutant. (C) The free energy surface of noninteracting two domains, F0(x, y), where x(y) is the number of residues that take the native configuration in domain I(II). (D) The differences in free energy between the connected two-domain protein and the separated two noninteracting domains, U(x, y), for the wild type. (E) U(x, y), for the circular permutant. (F) The difference in free energy between the wild type and the mutant, FwildFmutant. ε/kBT = 0.53 and σ = 1.5kB.