Computational Analysis of the Soluble Form of the Intracellular Chloride Ion Channel Protein CLIC1
Figure 2
Time course of conformational changes in the apo and covalently ligand-bound simulations. Data from the apo1 simulation are in the left panels and those from the cov1 simulation are in the right panels. All measurements were taken at 150 ps intervals. (a) RMS deviation of C atoms from the starting structure (not including residues 1–5 or 146–165). (b) Projection of PCA EV1 from the C trajectory (not including residues 145–165). (c) Backbone dihedral angle of residue Asn23. (d) Backbone dihedral angles of residues 194 (blue), 195 (red), 197 (black), and 198 (green). (e) Distance between the hydroxyl oxygen of Tyr233 and the sulfur atom of Cys24 (green) and moving average over 20 150 ps intervals of distance between the hydroxyl oxygen of Tyr233 and the side chain -carbon atom of Cys24 (red).
