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.
Biochem Biophys Res Commun. 2010 Jan 29;392(1):95-9. doi: 10.1016/j.bbrc.2010.01.003. Epub 2010 Jan 7.
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.
提出了一种不依赖于实验蛋白质结构信息的计算方法，用于从水动力学研究中识别蛋白质折叠中的关键残基。基于全原子分子动力学模拟，在 Trp-cage 蛋白折叠过程中识别出两个具有明显水动力行为的关键残基。研究表明，所鉴定的关键残基在 3D 结构和疏水性诱导折叠中都起着至关重要的作用。通过观察关键残基周围的水化水动力学，可以解释折叠的动力学途径。
