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

doi:10.1088/1674-1056/24/1/018201

中国物理B ›› 2015, Vol. 24 ›› Issue (1): 18201-018201.doi: 10.1088/1674-1056/24/1/018201

所属专题： TOPICAL REVIEW — Ultrafast intense laser science

• TOPICAL REVIEW—Ultrafast intense laser science • 上一篇下一篇

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

高光宇^a, 李渝^a, 王伟^a, 王树峰^a, Dongping Zhong^b, 龚旗煌^{a c}

a Institute of Modern Optics & State Key Laboratory for Artificial Microstructure and Mesoscopic Physics, School of Physics, Peking University, Beijing 100871, China;
b Departments of Physics, Chemistry and Biochemistry, Programs of Biophysics, Chemical Physics and Biochemistry, The Ohio State University, Columbus, OH 43210, USA;
c Collaborative Innovation Center of Quantum Matter, Beijing 100190, China

收稿日期:2014-10-22 修回日期:2014-12-01 出版日期:2015-01-05 发布日期:2015-01-05
基金资助:
Project supported by the National Basic Research Program of China (Grant Nos. 2013CB921904, 2009CB930504, and 2013CB328700) and the National Natural Science Foundation of China (Grant Nos. 11074016, 11121091, 10934001, 61177020，11134001, and 10828407).

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

Gao Guang-Yu (高光宇)^a, Li Yu (李渝)^a, Wang Wei (王伟)^a, Wang Shu-Feng (王树峰)^a, Dongping Zhong^b, Gong Qi-Huang (龚旗煌)^{a c}

a Institute of Modern Optics & State Key Laboratory for Artificial Microstructure and Mesoscopic Physics, School of Physics, Peking University, Beijing 100871, China;
b Departments of Physics, Chemistry and Biochemistry, Programs of Biophysics, Chemical Physics and Biochemistry, The Ohio State University, Columbus, OH 43210, USA;
c Collaborative Innovation Center of Quantum Matter, Beijing 100190, China

Received:2014-10-22 Revised:2014-12-01 Online:2015-01-05 Published:2015-01-05
Contact: Wang Shu-Feng E-mail:wangsf@pku.edu.cn
Supported by:
Project supported by the National Basic Research Program of China (Grant Nos. 2013CB921904, 2009CB930504, and 2013CB328700) and the National Natural Science Foundation of China (Grant Nos. 11074016, 11121091, 10934001, 61177020，11134001, and 10828407).

摘要/Abstract

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.

关键词: ultrafast spectroscopy, protein dynamics, staphylococcal nuclease (SNase), site-directed mutagenesis

Abstract:

Key words: ultrafast spectroscopy, protein dynamics, staphylococcal nuclease (SNase), site-directed mutagenesis

中图分类号: (Femtosecond probing of biological molecules)

82.53.Ps

87.14.E- (Proteins) 87.15.kr (Protein-solvent interactions) 87.64.K- (Spectroscopy)

高光宇, 李渝, 王伟, 王树峰, Dongping Zhong, 龚旗煌. Ultrafast solvation dynamics at internal sites of staphylococcal nuclease investigated by site-directed mutagenesis[J]. 中国物理B, 2015, 24(1): 18201-018201.

Gao Guang-Yu (高光宇), Li Yu (李渝), Wang Wei (王伟), Wang Shu-Feng (王树峰), Dongping Zhong, Gong Qi-Huang (龚旗煌). Ultrafast solvation dynamics at internal sites of staphylococcal nuclease investigated by site-directed mutagenesis[J]. Chin. Phys. B, 2015, 24(1): 18201-018201.

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

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

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