| Literature DB >> 33439619 |
Yunfei Hu1,2, Kai Cheng1, Lichun He1,2, Xu Zhang1,2, Bin Jiang1,2, Ling Jiang1,2, Conggang Li1,2, Guan Wang1,2, Yunhuang Yang1,2, Maili Liu1,2.
Abstract
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.Year: 2021 PMID: 33439619 DOI: 10.1021/acs.analchem.0c03830
Source DB: PubMed Journal: Anal Chem ISSN: 0003-2700 Impact factor: 6.986