Ultrafast solvation dynamics at internal sites of staphylococcal nuclease investigated by site-directed mutagenesis

作     者：高光宇 李渝 王伟 王树峰 Dongping Zhong 龚旗煌 

作者机构：Institute of Modern Optics & State Key Laboratory for Artificial Microstructure and Mesoscopic PhysicsSchool of PhysicsPeking University Departments of PhysicsChemistry and BiochemistryPrograms of BiophysicsChemical Physics and BiochemistryThe Ohio State UniversityColumbusOH 43210USA Collaborative Innovation Center of Quantum Matter 

出 版 物：《Chinese Physics B》 (中国物理B（英文版）)

年 卷 期：2015年第24卷第1期

页      面：81-88页

核心收录：

学科分类：0710[理学-生物学] 071010[理学-生物化学与分子生物学] 07[理学] 

基　　金：Project supported by the National Basic Research Program of China(Grant Nos.2013CB921904,2009CB930504,and 2013CB328700) the National Natural Science Foundation of China(Grant Nos.11074016,11121091,10934001,61177020,11134001,and 10828407) 

主　　题：ultrafast spectroscopy protein dynamics staphylococcal nuclease(SNase) site-directed mutagenesis 

摘      要：Internal solvation of protein was studied by site-directed mutagenesis, with which an intrinsically fluorescent probe,tryptophan, is inserted into the desired position inside a protein molecule for ultrafast spectroscopic study. Here we review this unique method for protein dynamics research. We first introduce the frontiers of protein solvation, site-directed mutagenesis, protein stability and characteristics, and the spectroscopic methods. Then we present time-resolved spectroscopic dynamics of solvation dynamics inside cavities of active sites. The studies are carried out on a globular protein, staphylococcal nuclease. The solvation at sites inside the protein molecule＇s cavities clearly reveals characteristics of the local environment. These solvation behaviors are directly correlated to enzyme activity.