Literature DB >> 33439619

NMR-Based Methods for Protein Analysis.

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


  1 in total

1.  Label-Free Fluorescence Molecular Beacon Probes Based on G-Triplex DNA and Thioflavin T for Protein Detection.

Authors:  Jun Xue; Jintao Yi; Hui Zhou
Journal:  Molecules       Date:  2021-05-17       Impact factor: 4.411

  1 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.