Please use this identifier to cite or link to this item: https://doi.org/10.1002/anie.200503558
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dc.titleSequence-specific assignment of aromatic resonances of uniformly 13C,15N-labeled proteins by using 13C- and 15N-Edited NOESY spectra
dc.contributor.authorLin, Z.
dc.contributor.authorXu, Y.
dc.contributor.authorYang, S.
dc.contributor.authorYang, D.
dc.date.accessioned2014-10-27T08:39:29Z
dc.date.available2014-10-27T08:39:29Z
dc.date.issued2006-03-13
dc.identifier.citationLin, Z., Xu, Y., Yang, S., Yang, D. (2006-03-13). Sequence-specific assignment of aromatic resonances of uniformly 13C,15N-labeled proteins by using 13C- and 15N-Edited NOESY spectra. Angewandte Chemie - International Edition 45 (12) : 1960-1963. ScholarBank@NUS Repository. https://doi.org/10.1002/anie.200503558
dc.identifier.issn14337851
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/101650
dc.description.abstract(Figure Presented) NOESY neighbors: A single 3D 13C- and 15N-edited NOESY experiment can be used to assign aromatic side-chain resonance signals of 13C,15N-labeled proteins on the basis of prior assignments of the signals of backbone and aliphatic side-chain groups. This strategy will improve the precision of protein structures, especially of large proteins. © 2006 Wiley-VCH Verlag GmbH & Co. KGaA.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1002/anie.200503558
dc.sourceScopus
dc.subjectNMR spectroscopy
dc.subjectProtein structures
dc.subjectProteins
dc.subjectSpectroscopic methods
dc.subjectStructure elucidation
dc.typeArticle
dc.contributor.departmentBIOLOGICAL SCIENCES
dc.description.doi10.1002/anie.200503558
dc.description.sourcetitleAngewandte Chemie - International Edition
dc.description.volume45
dc.description.issue12
dc.description.page1960-1963
dc.description.codenACIEA
dc.identifier.isiut000236119000032
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