Correlated motions in native proteins from MS analysis of NH exchange: Evidence for a manifold of unfolding reactions in ovomucoid third domain

被引：41

作者：

Arrington, CB

Robertson, AD ^{[1
]}

机构：

[1] Univ Iowa, Dept Biochem, Iowa City, IA 52242 USA

[2] Univ Iowa, Med Sci Training Program, Iowa City, IA 52242 USA

来源：

JOURNAL OF MOLECULAR BIOLOGY | 2000年 / 300卷 / 01期

关键词：

ensembles; protein unfolding; hydrogen exchange; electrospray mass spectrometry; ovomucoid third domain;

D O I：

10.1006/jmbi.2000.3859

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：

Native-state amide hydrogen exchange monitored by NMR spectroscopy and mass spectrometry (MS) has the potential to provide detailed residue-level information regarding correlated motions occurring on the microseconds to seconds timescale. To expand the applicability of MS to these studies, a new algorithm has been developed to interpret MS data for exchange occurring between the EX2 and EX1 kinetic limits. Re-interpretation of MS data for ovomucoid third domain multiple unfolding or partial unfolding reactions limits reveals (C) 2000 Academic Press.

引用

收藏

页码：221 / 232

页数：12

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