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. Author manuscript; available in PMC: 2014 Jul 9.
Published in final edited form as: J Chem Theory Comput. 2013 Jun 10;9(7):3072–3083. doi: 10.1021/ct400315q

Figure 8. Cancellation of effects in solvent and in the protein buffers the overall ΔGBind to changes in parameters.

Figure 8

In CCP (top, red), ΔΔGWat buffers 35–50% of the change in ΔΔGComplex (despite slopes of 0.6–0.7), while in Gyrase (bottom, blue) this buffering is even stronger. Best fit lines are shown in black. Slope uncertainties represent one standard deviation from bootstrapping calculations.