Fig. 3
From: Topological determinants in protein folding dynamics: a comparative analysis of metamorphic proteins
Comparative analysis on the pH-dependent folding behavior of B4 and Sb3. (A) Chevron plots of B4 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 B4 versus pH. The fit clearly reveals the presence of two monotonic sigmoidal transitions over pH 7 and below pH 4.5, respectively. (C) Chevron plots of Sb3 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 Sb3, 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