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|Title:||Resolution-enhanced 4D 15N/13C NOESY protein NMR spectroscopy by application of the covariance transform||Authors:||Snyder, D.A.
|Issue Date:||21-Nov-2007||Citation:||Snyder, 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||Abstract:||The 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.||Source Title:||Journal of the American Chemical Society||URI:||http://scholarbank.nus.edu.sg/handle/10635/101573||ISSN:||00027863||DOI:||10.1021/ja075533n|
|Appears in Collections:||Staff Publications|
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