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

被引:5
作者
Gao Guang-Yu [1 ,2 ]
Li Yu [1 ,2 ]
Wang Wei [1 ,2 ]
Wang Shu-Feng [1 ,2 ]
Zhong, Dongping [3 ,4 ,5 ,6 ]
Gong Qi-Huang [1 ,2 ,7 ]
机构
[1] Peking Univ, Sch Phys, Inst Modern Opt, Beijing 100871, Peoples R China
[2] Peking Univ, Sch Phys, State Key Lab Artificial Microstruct & Mesoscop P, Beijing 100871, Peoples R China
[3] Ohio State Univ, Dept Phys, Program Biophys, Columbus, OH 43210 USA
[4] Ohio State Univ, Dept Chem & Biochem, Program Biophys, Columbus, OH 43210 USA
[5] Ohio State Univ, Dept Phys, Program Chem Phys & Biochem, Columbus, OH 43210 USA
[6] Ohio State Univ, Dept Chem & Biochem, Program Chem Phys & Biochem, Columbus, OH 43210 USA
[7] Collaborat Innovat Ctr Quantum Matter, Beijing 100190, Peoples R China
基金
中国国家自然科学基金;
关键词
ultrafast spectroscopy; protein dynamics; staphylococcal nuclease (SNase); site-directed mutagenesis; MOLECULAR-DYNAMICS; HYDRATION DYNAMICS; WATER PENETRATION; PROTEIN; INTERIOR; FLUORESCENCE; FEMTOSECOND; STABILITY; NMR; FOLDABILITY;
D O I
10.1088/1674-1056/24/1/018201
中图分类号
O4 [物理学];
学科分类号
0702 ;
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.
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收藏
页数:8
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