A general strategy for the assignment of aliphatic side-chain resonances of uniformly 13C, 15N-labeled large proteins

Please use this identifier to cite or link to this item: https://doi.org/10.1021/ja053539b

Title:	A general strategy for the assignment of aliphatic side-chain resonances of uniformly 13C, 15N-labeled large proteins
Authors:	Xu, Y. Lin, Z. Ho, C. Yang, D.
Issue Date:	31-Aug-2005
Citation:	Xu, 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
Abstract:	A 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.
Source Title:	Journal of the American Chemical Society
URI:	http://scholarbank.nus.edu.sg/handle/10635/99835
ISSN:	00027863
DOI:	10.1021/ja053539b
Appears in Collections:	Staff Publications

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