Please use this identifier to cite or link to this item: https://doi.org/10.1021/ja710477h
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dc.titleAccurately probing slow motions on millisecond timescales with a robust NMR relaxation experiment
dc.contributor.authorLong, D.
dc.contributor.authorLiu, M.
dc.contributor.authorYang, D.
dc.date.accessioned2014-10-27T08:20:53Z
dc.date.available2014-10-27T08:20:53Z
dc.date.issued2008-02-27
dc.identifier.citationLong, D., Liu, M., Yang, D. (2008-02-27). Accurately probing slow motions on millisecond timescales with a robust NMR relaxation experiment. Journal of the American Chemical Society 130 (8) : 2432-2433. ScholarBank@NUS Repository. https://doi.org/10.1021/ja710477h
dc.identifier.issn00027863
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/99999
dc.description.abstractA new pulse scheme is proposed for the accurate measurement of relaxation dispersion, which cycles the phases of CPMG pulses. Numerical simulations show that systematic errors in the measured relaxation rates mainly result from off-resonance and radio frequency inhomogeneity effects and they can be significantly suppressed with the method proposed here. The method has been demonstrated on human liver fatty acid binding protein. It allows the reliable identification of residues undergoing conformational exchange on millisecond timescales and accurate extraction of kinetics parameters. The relaxation dispersion data indicate that human liver fatty acid binding protein is highly flexible on millisecond timescales. Copyright © 2008 American Chemical Society.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1021/ja710477h
dc.sourceScopus
dc.typeArticle
dc.contributor.departmentBIOLOGICAL SCIENCES
dc.description.doi10.1021/ja710477h
dc.description.sourcetitleJournal of the American Chemical Society
dc.description.volume130
dc.description.issue8
dc.description.page2432-2433
dc.description.codenJACSA
dc.identifier.isiut000253400900030
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