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. Author manuscript; available in PMC: 2009 Feb 22.
Published in final edited form as: J Mol Biol. 2007 Dec 14;376(3):827–838. doi: 10.1016/j.jmb.2007.12.016

Figure 2.

Figure 2

Conformational flexibility of the C-terminal domain of p27 in the p27/Cdk2/cyclin A complex. Superposition of p27/Cdk2/cyclin A structures at varying time intervals during a 12.7 ns molecular dynamics simulation (5 ns – magenta, 6.1 ns – yellow, 7.2 ns – light green, 8.3 ns – cyan, 9.4 – blue, 10.5 ns – orange, 11.6 ns – red, 12.7 ns – dark green). The solvent accessible surface for Cdk2/cyclin A is colored grey. The figure was generated using the program PyMol. (b) Summary of average Ψ and φ torsion angle values for residues in the C-terminal domain of p27 over the course of the MD simulation. Error bars indicate RMSD values for Ψ and φ torsion angles during the simulation. (c) and (d) Electrostatic repulsion between the C-terminal region of p27 and the surface of the Cdk2/cyclin A complex. Electrostatic potential surface generated with the program MOLMOL49 for the (c) p27/Cdk2/cyclin A complex and (d) Cdk2/cyclin A complex where p27 is illustrated as a ribbon and is colored according to Figure 1. The structure shown was obtained at 8.3 ns during the MD trajectory.