共 15 条
Internal and Global Protein Motion Assessed with a Fusion Construct and In-Cell NMR Spectroscopy
被引:43
作者:

Barnes, Christopher O.
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机构:
Univ N Carolina, Dept Chem, Chapel Hill, NC 27599 USA Univ N Carolina, Dept Chem, Chapel Hill, NC 27599 USA

Monteith, William B.
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机构:
Univ N Carolina, Dept Chem, Chapel Hill, NC 27599 USA Univ N Carolina, Dept Chem, Chapel Hill, NC 27599 USA

Pielak, Gary J.
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h-index: 0
机构:
Univ N Carolina, Dept Chem, Chapel Hill, NC 27599 USA
Univ N Carolina, Dept Biochem & Biophys, Chapel Hill, NC 27599 USA Univ N Carolina, Dept Chem, Chapel Hill, NC 27599 USA
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:
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.
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收藏
页码:390 / 391
页数:2
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