Fig. 2.

Distal mutations affect the thermodynamics of binding and folding. (A) Apparent free energy (ΔG_app) of binding. The solid black line shows the fitted curve for the v142g ΔG data. The solid red lines represent the prediction of WT data based on the fitting of ΔH_conf,app. Lines represent the prediction, plus and minus the average standard error of determining ΔG_app. (Inset) Change in ΔG_app for each protein, with temperature, referenced from 27° C. ΔΔG_{27° C}(Temp) = ΔG(Temp) − ΔG(27° C). (B) Apparent enthalpy of binding (ΔH_app) Ap5A. (Inset) Corrected data and fitting functions representing −ΔH_conf,app (Eq. 2a). (C) Representative circular dichrosim thermal unfolding experiments (deg·cm²/dmol·res). Denatured state signals are normalized. Lines are fitting functions for a two-state thermodynamic model. (Table) Thermodynamic parameters determined from the two-state fits: a, van't Hoff enthalpy (kcal/mol) (at T_m); b, transition midpoint temperature (°C).