Correlated motions in native proteins from MS analysis of NH exchange: evidence for a manifold of unfolding reactions in ovomucoid third domain
Journal of Molecular BiologyPublished 1 June 2000
Cammon B. Arrington, Andrew D. Robertson
Citations52
SJR quartileQ1
SJR score2.21
SNIP1.13
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TL;DR
A new algorithm has been developed to interpret MS data for exchange occurring between the EX2 and EX1 kinetic limits, which reveals multiple unfolding or partial unfolding reactions of native-state amide hydrogen exchange.
Abstract
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 reveals multiple unfolding or partial unfolding reactions.
Keywords
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