Nullspace Sampling with Holonomic Constraints Reveals Molecular Mechanisms of Protein Gαs
Fig 8
Heatmaps of conformational variability.
a) RMS fluctuations of DoFs for KGS (red) and iMC (blue) for 20,000 samples starting from the activated conformation (top two panels, orange) and the inactive conformation (bottom two panels, grey). The DoFs corresponding to the AH-domain and helix α5 are colored in darker shades. Free DoFs are circles, cycle DoFs are squares. The horizontal lines correspond to the mean RMSF value of the DoFs plus 2σ. b,c) Heatmaps representing the contribution of DoFs to conformational variability for KGS (b) and iMC (c). Coupling in the GDP binding pocket (red circle, α5, α1, and the adjacent β1–α1 loop (P-loop)) extends to include helix αF (bottom of the red circle), Linker II (SW I), and the N-terminus of αE (right side of the blue oval).