Internal and Global Protein Motion Assessed with a Fusion Construct and In-Cell NMR Spectroscopy

被引：43

作者：

Barnes, Christopher O. ^{[1
]}

Monteith, William B. ^{[1
]}

Pielak, Gary J. ^{[1
,2
]}

机构：

[1] Univ N Carolina, Dept Chem, Chapel Hill, NC 27599 USA

[2] Univ N Carolina, Dept Biochem & Biophys, Chapel Hill, NC 27599 USA

来源：

CHEMBIOCHEM | 2011年 / 12卷 / 03期

基金：

美国国家卫生研究院; 美国国家科学基金会;

关键词：

disordered proteins; globular proteins; NMR spectroscopy; protein dynamics; protein stability; ESCHERICHIA-COLI; ALPHA-SYNUCLEIN; DIFFUSION;

D O I：

10.1002/cbic.201000610

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：

Motion study: We have examined a fusion protein comprising a globular (ubiquitin) and an intrinsically disordered (α-synuclein) component. The data show that internal motion determines the quality of in-cell NMR spectra. The disordered component exhibits a high-resolution spectrum, whereas the globular portion is only observed when the cells are lysed and diluted. © 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

引用

页码：390 / 391

页数：2