Water dynamics clue to key residues in protein folding.
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.
Gao
Meng
M
State Key Laboratory for Turbulence and Complex Systems, and Department of Biomedical Engineering, and Center for Theoretical Biology, and Center for Protein Science, Peking University, Beijing 100871, China.
Zhu
Huaiqiu
H
Yao
Xin-Qiu
XQ
She
Zhen-Su
ZS
D000596:Amino Acids / Q000737:chemistry*; D019277:Entropy; D008956:Models, Chemical; D056004:Molecular Dynamics Simulation; D011487:Protein Conformation; D017510:Protein Folding; D014867:Water / Q000737:chemistry*
D000596:Amino Acids; D014867:Water