Mapping the Structural and Dynamical Features of Kinesin Motor Domains
Figure 4
Time evolution of local and global structural changes.
(A) The protrusion angle of α4 relative to β3. Dashed lines depict the average angle for ATP-like (red) and ADP-like (green) crystallographic structures. (B) The secondary structure content of SI and (C) SII-α4. Yellow represents beta strand, blue alpha helix, and white coil secondary structure types (see text for details). (D) Contact formation and breaking activity during nucleotide free simulations. The plot reports the contact formation events (green), the contact breaking events (red) and total events (gray, formation + breaking) as a function of simulation time.