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NMR-Based Methods for Protein Analysis
Author(s) -
Yunfei Hu,
Kai Cheng,
Lichun He,
Xu Zhang,
Bin Jiang,
Ling Jiang,
Conggang Li,
Guan Wang,
Yunhuang Yang,
Maili Liu
Publication year - 2021
Publication title -
analytical chemistry
Language(s) - Uncategorized
Resource type - Journals
SCImago Journal Rank - 2.117
H-Index - 332
eISSN - 1520-6882
pISSN - 0003-2700
DOI - 10.1021/acs.analchem.0c03830
Subject(s) - chemistry , nuclear magnetic resonance spectroscopy , solid state nuclear magnetic resonance , structural biology , protein dynamics , protein structure , nanotechnology , biophysics , computational biology , biochemistry , nuclear magnetic resonance , physics , materials science , organic chemistry , biology
Nuclear magnetic resonance (NMR) spectroscopy is a well-established method for analyzing protein structure, interaction, and dynamics at atomic resolution and in various sample states including solution state, solid state, and membranous environment. Thanks to rapid NMR methodology development, the past decade has witnessed a growing number of protein NMR studies in complex systems ranging from membrane mimetics to living cells, which pushes the research frontier further toward physiological environments and offers unique insights in elucidating protein functional mechanisms. In particular, in-cell NMR has become a method of choice for bridging the huge gap between structural biology and cell biology. Herein, we review the recent developments and applications of NMR methods for protein analysis in close-to-physiological environments, with special emphasis on in-cell protein structural determination and the analysis of protein dynamics, both difficult to be accessed by traditional methods.

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