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.
引用
收藏
页数:8
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