Fig. 3
From: Protein conformational flexibility modulates kinetics and thermodynamics of drug binding
Thermodynamic profiles of N-HSP90 inhibitors measured by ITC. The enthalpic and entropic components of the binding free energy are shown in a and b for for WT N-HSP90, and the L107A mutant, respectively. The dashed diagonal line (ΔH=−TΔS) divides the plot into two main areas where the enthalpy (gray) or the entropy (red) dominate the binding free energy (ΔG). Compounds 1–6 are loop binders and are colored black and compounds 7–20 are helix-binders and are colored red. c, d Isothermal titration calorimetry fitting curves for compounds 1 (c) and 16 (d) bound to WT N-HSP90 (full circles) and to the L107A mutant (open circles) with thermodynamic parameters shown in the respective tables. e Box plot showing the difference in the enthalpy (ΔΔH), entropy (Δ(−TΔS)) and binding free energy (ΔΔG) for L07A relative to WT for loop- (colored black) and helix-binders (colored red). The boxes denote the 25th and 75th percentiles and the error bars the 5th and 95th percentiles
