Figure 4

(A) Reweight of the Free Energy along the distance between the sulfur atoms of residues Cys60 and Cys65 (Tyr65 in the WT). The population of structures with a low distance between the two residues is increased in the Y65C mutant, with values as low as 4 Å in the unfolded state (CMAP < 5) of both proteins. (B) Free Energy of the Y65C mutant with and without the disulphide bridge between Cys60 and Cys65 as a function of the contact map.