Please use this identifier to cite or link to this item: https://doi.org/10.1021/ja075533n
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dc.titleResolution-enhanced 4D 15N/13C NOESY protein NMR spectroscopy by application of the covariance transform
dc.contributor.authorSnyder, D.A.
dc.contributor.authorXu, Y.
dc.contributor.authorYang, D.
dc.contributor.authorBrüschweiler, R.
dc.date.accessioned2014-10-27T08:38:39Z
dc.date.available2014-10-27T08:38:39Z
dc.date.issued2007-11-21
dc.identifier.citationSnyder, D.A., Xu, Y., Yang, D., Brüschweiler, R. (2007-11-21). Resolution-enhanced 4D 15N/13C NOESY protein NMR spectroscopy by application of the covariance transform. Journal of the American Chemical Society 129 (46) : 14126-14127. ScholarBank@NUS Repository. https://doi.org/10.1021/ja075533n
dc.identifier.issn00027863
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/101573
dc.description.abstractThe combination of shared-evolution 4D 15N/13C-edited NOESY spectroscopy with covariance NMR is introduced, which yields, as a sub-spectrum, an asymmetric 4D 15N/13C-edited NOESY spectrum at a resolution enhanced 5-fold over the one of a non-shared 4D 15N/13C-edited NOESY measured with the same sweep widths and number of increments. The achieved resolution enhancement allows for a substantial increase in the number of assigned NOEs over that of the 4D Fourier transform spectrum and should prove useful for efficient, high-resolution NMR-based studies of protein structure. Copyright © 2007 American Chemical Society.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1021/ja075533n
dc.sourceScopus
dc.typeArticle
dc.contributor.departmentBIOLOGICAL SCIENCES
dc.description.doi10.1021/ja075533n
dc.description.sourcetitleJournal of the American Chemical Society
dc.description.volume129
dc.description.issue46
dc.description.page14126-14127
dc.description.codenJACSA
dc.identifier.isiut000251182000011
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