Fig. 5
From: Topological determinants in protein folding dynamics: a comparative analysis of metamorphic proteins
Analysis of the pH-dependent folding behavior of the Sb4 variant. (A) Chevron plots of the Sb4_B-fold population measured from pH 2.5 to pH 9.0. Lines are the best global fit to a two-state equation with shared m-values. (B) Logarithm of the unfolding equilibrium constants between the native and denatured state of Sb4_B-fold versus pH. The fit clearly reveals the presence of a single, monotonic sigmoidal transition over pH 7.5 (C) Chevron plots of the Sb4_S-fold population measured from pH 2.5 to pH 9.0. Lines are the best global fit to a three-state equation with shared m-values. (D) Logarithm of the partition factor KI of Sb4_S-fold, proportional to the difference between the activation barriers for the pre-equilibrium intermediate state to revert to the denatured state rather than proceeding to the native state, versus pH