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

ISSN号：1674-1056
期刊名称：《中国物理B：英文版》
时间：0
分类：Q516[生物学—生物化学] Q78[生物学—分子生物学]
作者机构：[1]Institute of Modern Optics & State Key Laboratory for Artificial Microstructure and Mcsoscopic Physics, School of Physics, Peking University, Beijing 100871, China, [2]Departments of Physics, Chemistry and Biochemistry, Programs of Biophysics, Chemical Physics and Biochemistry, The Ohio State University, Columbus, 0/-/43210, USA, [3]Collaborative Innovation Center of Quantum Matter, Beijing 100190, China
相关基金：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）Acknowledgements The wild type （WT） SNase plasmid was generously provided by Prof. Bertrand Garcia-Moreno （Johns Hopkins University）. We very much appreciate Dr. Lijuan Wang （Ohio State University） directing us in preparing all the mutants and setting up the biological lab.

作者：高光宇[1], 李渝[1], 王伟[1], 王树峰[1], Dongping Zhong[2], 龚旗煌[1,3]

关键词：葡萄球菌核酸酶, 定点诱变, 溶剂化, 动力学, 金黄色, 蛋白质分子, 站点, 时间分辨光谱, ultrafast spectroscopy, protein dynamics, staphylococcal nuclease（SNase）, site-directed mutagenesis

中文摘要：

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.

英文摘要：

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.