Characterisation of protein unfolding by NMR diffusion measurements

被引：194

作者：

Jones, JA ^{[1
]}

Wilkins, DK ^{[1
]}

Smith, LJ ^{[1
]}

Dobson, CM ^{[1
]}

机构：

[1] UNIV OXFORD,OXFORD CTR MOL SCI,NEW CHEM LAB,OXFORD OX1 3QT,ENGLAND

来源：

JOURNAL OF BIOMOLECULAR NMR | 1997年 / 10卷 / 02期

基金：

英国工程与自然科学研究理事会; 英国医学研究理事会; 英国生物技术与生命科学研究理事会;

关键词：

protein folding; non-native states; hydrodynamic radius; lysozyme;

D O I：

10.1023/A:1018304117895

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：

The characterisation of non-native stales of proteins is a key problem in studies of protein folding. Complete characterisation of these states requires a description of both local and global properties, including molecular dimensions. Here we present results from pulsed field gradient experiments designed to compare the effective hydrodynamic radii of a protein in native and non-native states. Measurements performed on lysozyme indicate that the effective hydrodynamic radius increases by 38+/-1% on unfolding in urea, a result completely consistent with a recent study by small-angle X-ray scattering.

引用

页码：199 / 203

页数：5

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