15N resonance assignments of oxidized and reduced Chromatium vinosum high-potential iron protein.
作者信息
Li D, Cottrell C E, Cowan J A
机构信息
Evans Laboratory of Chemistry, Ohio State University, Columbus 43210, USA.
出版信息
J Protein Chem. 1995 Apr;14(3):115-26. doi: 10.1007/BF01980323.
PMID:7576079
Abstract
The 15N resonances in reduced and oxidized Chromatium vinosum high-potential iron protein have been assigned by use of 1H-1H COSY spectra and 1H-15N HMQC. HMQC-COSY, and HMQC-NOESY spectra. Unambiguous assignment of 70 of 85 backbone 15N resonances in the reduced protein and 62 of 85 resonances in the oxidized protein are made, as are 12 of 21 side-chain 15N resonances.
摘要
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