Please use this identifier to cite or link to this item: https://doi.org/10.1021/ja053539b
DC FieldValue
dc.titleA general strategy for the assignment of aliphatic side-chain resonances of uniformly 13C, 15N-labeled large proteins
dc.contributor.authorXu, Y.
dc.contributor.authorLin, Z.
dc.contributor.authorHo, C.
dc.contributor.authorYang, D.
dc.date.accessioned2014-10-27T08:19:07Z
dc.date.available2014-10-27T08:19:07Z
dc.date.issued2005-08-31
dc.identifier.citationXu, Y., Lin, Z., Ho, C., Yang, D. (2005-08-31). A general strategy for the assignment of aliphatic side-chain resonances of uniformly 13C, 15N-labeled large proteins. Journal of the American Chemical Society 127 (34) : 11920-11921. ScholarBank@NUS Repository. https://doi.org/10.1021/ja053539b
dc.identifier.issn00027863
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/99835
dc.description.abstractA general strategy is proposed to assign aliphatic side-chain resonances of large 13C,15N-labeled proteins without deuteration, using 4D 13C,15N-edited NOESY and MQ-(H)CCH-TOCSY experiments on the basis of prior assignments of backbone and 13Cβ resonances. The strategy has been tested on a 214 residue protein (DdCAD-1) and applied to a chain-selectively 13C,15N-labeled hemoglobin (65 kDa). About 96 and 80% aliphatic side-chain spins in DdCAD-1 and hemoglobin have been assigned, respectively. The strategy proposed here will be very useful for the structure determination and dynamics characterization of large proteins by NMR. Copyright © 2005 American Chemical Society.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1021/ja053539b
dc.sourceScopus
dc.typeArticle
dc.contributor.departmentBIOLOGICAL SCIENCES
dc.description.doi10.1021/ja053539b
dc.description.sourcetitleJournal of the American Chemical Society
dc.description.volume127
dc.description.issue34
dc.description.page11920-11921
dc.description.codenJACSA
dc.identifier.isiut000231605900021
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