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|Title:||A general strategy for the assignment of aliphatic side-chain resonances of uniformly 13C, 15N-labeled large proteins|
|Authors:||Xu, Y. |
|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|
|Appears in Collections:||Staff Publications|
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