MOLECULAR-DYNAMICS OF THE H-RAS GENE-ENCODED P21 PROTEIN - IDENTIFICATION OF FLEXIBLE REGIONS AND POSSIBLE EFFECTOR DOMAINS

We previously reported a complete computer-based three-dimensional structure for residues 1-171 of the Gly 12-containing ras-gene-encoded p21 protein complexed with GDP. This structure was subsequently shown to closely agree with a high-resolution x-ray crystallographic structure of p21. In this communication, we report a molecular dynamics simulation of the modelled structure in an explicit shell of water molecules to identify domains within the protein that are unusually flexible. These domains represent regions which are most likely to