Protein dynamics in living cells studied by in-cell NMR spectroscopy

被引：34

作者：

Li, Conggang ^{[1
]}

Liu, Maili ^{[1
]}

机构：

[1] Chinese Acad Sci, Key Lab Magnet Resonance Biol Syst, State Key Lab Magnet Resonance & Mol & Atom Phys, Wuhan Ctr Magnet Resonance,Wuhan Inst Phys & Math, Wuhan 430072, Peoples R China

来源：

FEBS LETTERS | 2013年 / 587卷 / 08期

关键词：

In-cell NMR; Protein dynamic; NUCLEAR-MAGNETIC-RESONANCE; SOLID-STATE NMR; GREEN FLUORESCENT PROTEIN; MODEL-FREE APPROACH; ROTATIONAL DIFFUSION; DISORDERED PROTEIN; F-19; NMR; RELAXATION; MEMBRANES; MOBILITY;

D O I：

10.1016/j.febslet.2012.12.023

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Most proteins function in cells where protein concentrations can reach 400 g/l. However, most quantitative studies of protein properties are performed in idealized, dilute conditions. Recently developed in-cell NMR techniques can provide protein structure and other biophysical properties inside living cells at atomic resolution. Here we review how protein dynamics, including global and internal motions have been characterized by in-cell NMR, and then discuss the remaining challenges and future directions. (C) 2013 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.

引用

页码：1008 / 1011

页数：4

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