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Slow motions in nondeuterated proteins: Concerted chemical shift modulations of backbone nuclei
Journal article   Peer reviewed

Slow motions in nondeuterated proteins: Concerted chemical shift modulations of backbone nuclei

J Wist, C Perazzolo and G Bodenhausen
Applied magnetic resonance, Vol.29(2), pp.251-259
2005

Abstract

Slow Motion Amide Proton Dipolar Contribution Conformational Exchange Isotropic Chemical Shift
A simple method designed to measure autorelaxation rates of double- and zero-quantum coherences DQC/ZQC{C'N} involving a carbonyl C' and the neighboring amide N nucleus in protein backbones provides valuable insight into slow motions in spite of interference both from the attached amide proton HI and from remote protons such as H-alpha in nondeuterated proteins. The method has been applied to human ubiquitin.

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Collaboration types
Domestic collaboration
International collaboration
Citation topics
2 Chemistry
2.123 Protein Stucture, Folding & Modelling
2.123.248 Solid-State NMR
Web Of Science research areas
Physics, Atomic, Molecular & Chemical
Spectroscopy
ESI research areas
Chemistry
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