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

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 fir...

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Bibliographic Details
Published in:Chinese physics B 2015, Vol.24 (1), p.81-88
Main Author: 高光宇 李渝 王伟 王树峰 Dongping Zhong 龚旗煌
Format: Article
Language:English
Subjects:
Dynamic tests
Dynamics
Fluorescence
Holes
Nuclease
Proteins
Solvation
Spectroscopy
动力学
定点诱变
时间分辨光谱
溶剂化
站点
葡萄球菌核酸酶
蛋白质分子
金黄色
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Summary: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.
ISSN:1674-1056
2058-3834
1741-4199
DOI:10.1088/1674-1056/24/1/018201