Gao M.,Center for Theoretical Biology |
Zhu H.,Center for Theoretical Biology |
Yao X.-Q.,Center for Theoretical Biology |
Yao X.-Q.,Kyoto University |
She Z.-S.,Center for Theoretical Biology
Biochemical and Biophysical Research Communications | Year: 2010
A computational method independent of experimental protein structure information is proposed to recognize key residues in protein folding, from the study of hydration water dynamics. Based on all-atom molecular dynamics simulation, two key residues are recognized with distinct water dynamical behavior in a folding process of the Trp-cage protein. The identified key residues are shown to play an essential role in both 3D structure and hydrophobic-induced collapse. With observations on hydration water dynamics around key residues, a dynamical pathway of folding can be interpreted. © 2010 Elsevier Inc. All rights reserved.