A general strategy for the assignment of aliphatic side-chain resonances of uniformly 13C,15N-labeled large proteins |
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Authors: | Xu Yingqi Lin Zhi Ho Chien Yang Daiwen |
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Affiliation: | Department of Biological Sciences, National University of Singapore, 14 Science Drive 4, Singapore 117543. |
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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 13Cbeta 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. |
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