Figure 6: Shift of open/closed equilibrium in ATP-saturated M2 versus WT AKe.
From: Overlap between folding and functional energy landscapes for adenylate kinase conformational change

Normalized chemical shift perturbations in ATP- and Ap5A-bound states referenced to the apo states are calculated according to δω=0.2Δ15N+Δ1H (p.p.m.). (a) Correlation between ATP and Ap5A chemical shift perturbations for WT AKe. The best-fitted straight line (red) has a slope of 0.62±0.07 with an R coefficient of 0.97. In all, 20 residues were used in the analysis. Inset: positions of the residues analysed in WT and M2 are coloured gold on the open AKe structure. (b) Correlation between ATP and Ap5A chemical shift perturbations for the M2 variant. The best-fitted straight line (red) has a slope of 1.07±0.1 with an R coefficient of 0.97; 19 residues were used in the analysis.