Nullspace Sampling with Holonomic Constraints Reveals Molecular Mechanisms of Protein Gαs
Fig 6
Direction of displacement of the AH-domain.
a) Relative frequency of the angles between KGS and iMC average displacements for each Cα of the AH-domain in the inactive (grey) and active states (orange/yellow). The average AH-domain displacement is shifted by 50 to 60 degrees for the states between the two methods. b) Differences in the directions of the mean displacement of the center of geometry of the Gα AH-domain between the KGS (red) and iMC (blue) ensembles. c) Directionality of the CA displacements of the α5-helix in the KGS (red) and iMC (blue) ensembles in the active state (top) and inactive state (bottom). The motion in the KGS ensemble is directed from the inactive conformation of α5 to the active conformation. d) Superimposed Ras-domains from the KGS ensembles for the active state (yellow) and inactive (grey) states. The amplitude of the Ras-domain ensemble is limited, except for marked fluctuations of helices α4 and α5.