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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


Chun Tang


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


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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publisher="Zhejiang University Press & Springer",

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%A Qing-fen Yang
%A Chun Tang
%J Journal of Zhejiang University SCIENCE B
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%I Zhejiang University Press & Springer
%DOI 10.1631/jzus.B1900135

T1 - On the necessity of an integrative approach to understand protein structural dynamics
A1 - Qing-fen Yang
A1 - Chun Tang
J0 - Journal of Zhejiang University Science B
VL - 20
IS - 6
SP - 496
EP - 502
%@ 1673-1581
Y1 - 2019
PB - Zhejiang University Press & Springer
ER -
DOI - 10.1631/jzus.B1900135

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.



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


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