NMR characterization of a single-cysteine mutant of Escherichia coli thioredoxin and a covalent thioredoxin-peptide complex

Mei Fen Jeng, Martine T. Reymond, Linda L. Tennant, Arne Holmgren, H. Jane Dyson

研究成果: Article同行評審

13 引文 斯高帕斯(Scopus)

摘要

The mechanism of disulfide reduction by thioredoxin in the cell is thought to occur through the formation and subsequent destruction of a mixed- disulfide intermediate between thioredoxin and the substrate. In order to model the interaction, we have prepared a mutant of Escherichia coli thioredoxin where the second cysteine residue of the active site has been replaced by an alanine residue. A specific covalent complex has been prepared between the remaining cysteine-containing peptide. This paper describes the preparation and characterization off the mutant protein both free and in the peptide complex.

原文English
頁(從 - 到)299-308
頁數10
期刊European Journal of Biochemistry
257
發行號2
DOIs
出版狀態Published - 1998 十月 15

All Science Journal Classification (ASJC) codes

  • Biochemistry

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