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. 2000 Nov 7;97(24):12991–12996. doi: 10.1073/pnas.230243097

Figure 1.

Figure 1

Comparison of the effects of mutations on protein stability at the mitochondrial surface (A) and in the molten globule state in vitro (B). To simplify the comparison, destabilization energies are standardized, in A by dividing the destabilization energy of mutations at the mitochondrial surface (ΔΔGimport) by the destabilization energy of the same mutations measured for the native state in vitro, and in B by dividing the destabilization energy of mutations in the molten globule state by the destabilization energy of the same mutations in the native protein. Data for B were calculated from ref. 38.