| Literature DB >> 16117513 |
Yingqi Xu1, Zhi Lin, Chien Ho, Daiwen Yang.
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.Entities:
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Year: 2005 PMID: 16117513 DOI: 10.1021/ja053539b
Source DB: PubMed Journal: J Am Chem Soc ISSN: 0002-7863 Impact factor: 15.419