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CLC number: Q51

On-line Access: 2019-05-15

Received: 2019-03-15

Revision Accepted: 2019-03-31

Crosschecked: 2019-04-12

Cited: 0

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Citations:  Bibtex RefMan EndNote GB/T7714

 ORCID:

Chun Tang

https://orcid.org/0000-0001-6477-6500

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Journal of Zhejiang University SCIENCE B 2019 Vol.20 No.6 P.496-502

http://doi.org/10.1631/jzus.B1900135


On the necessity of an integrative approach to understand protein structural dynamics


Author(s):  Qing-fen Yang, Chun Tang

Affiliation(s):  Hubei Key Laboratory of Natural Medicinal Chemistry and Resource Evaluation, School of Pharmacy, Tongji Medical College, Huazhong University of Science and Technology, Wuhan 430030, China; more

Corresponding email(s):   tanglab@wipm.ac.cn

Key Words:  Conformational dynamics, Integrative structural biology, Distance restraint, Ensemble averaging, Nuclear magnetic resonance (NMR)


Qing-fen Yang, Chun Tang. On the necessity of an integrative approach to understand protein structural dynamics[J]. Journal of Zhejiang University Science B, 2019, 20(6): 496-502.

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doi="10.1631/jzus.B1900135"
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T1 - On the necessity of an integrative approach to understand protein structural dynamics
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Abstract: 
Proteins are dynamic, fluctuating between multiple conformational states. Protein dynamics, spanning orders of magnitude in time and space, allow proteins to perform specific functions. Moreover, under certain conditions, proteins can morph into a different set of conformations. Thus, a complete understanding of protein structural dynamics can provide mechanistic insights into protein function. Here, we review the latest developments in methods used to determine protein ensemble structures and to characterize protein dynamics. Techniques including X-ray crystallography, cryogenic electron microscopy, and small angle scattering can provide structural information on specific conformational states or on the averaged shape of the protein, whereas techniques including nuclear magnetic resonance, fluorescence resonance energy transfer (FRET), and chemical cross-linking coupled with mass spectrometry provide information on the fluctuation of the distances between protein domains, residues, and atoms for the multiple conformational states of the protein. In particular, FRET measurements at the single-molecule level allow rapid resolution of protein conformational states, where information is otherwise obscured in bulk measurements. Taken together, the different techniques complement each other and their integrated use can offer a clear picture of protein structure and dynamics.

整合方法研究蛋白质结构动态之必要性

概要:蛋白质是动态的,在多种结构状态间转化.蛋白质的结构动态在时间和空间上跨越多个数量级,允许蛋白质执行特定生物学功能.细胞条件和细胞环境的变化会使蛋白质动态结构发生变化.因此,对蛋白质结构动态的全面表征可提供对蛋白质功能的机制的深入了解.在这里,我们综述了用于测定蛋白质系综动态结构和表征蛋白质结构动态变化的方法的最新发展.X射线晶体学、冷冻电镜和小角散射等技术可提供关于蛋白质特定状态或平均的结构信息,而核磁共振、荧光共振能量转移(FRET)和化学交联质谱等技术则提供了蛋白质结构域、蛋白质残基和原子之间的处于不同结构状态时的距离波动信息.尤其要指出的是,单分子水平的FRET测量能对蛋白质构象状态进行快速区分,而这样的信息会在其它测量中被掩盖.总之,不同的生物物理技术互为补充,只有通过它们的综合运用,才能清晰可见蛋白质结构和动态.
关键词:结构动态;整合结构生物学;距离约束;系综平均;核磁共振

Darkslateblue:Affiliate; Royal Blue:Author; Turquoise:Article

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