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Special Issue:
TOPICAL REVIEW — Ultrafast intense laser science
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| TOPICAL REVIEW—Ultrafast intense laser science |
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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 Zhongb, 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 |
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Abstract 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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Received: 22 October 2014
Revised: 01 December 2014
Accepted manuscript online:
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PACS:
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82.53.Ps
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(Femtosecond probing of biological molecules)
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87.14.E-
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(Proteins)
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87.15.kr
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(Protein-solvent interactions)
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87.64.K-
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(Spectroscopy)
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| Fund: 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). |
Corresponding Authors:
Wang Shu-Feng
E-mail: wangsf@pku.edu.cn
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Cite this article:
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 2015 Chin. Phys. B 24 018201
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