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：
美国国家科学基金会; 美国国家卫生研究院;
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
收藏
页码：390 / 391
页数：2
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