NMR paper NMR characterization of a single-cysteine mutant of Escherichia coli thioredoxin and

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[NMR paper] NMR characterization of a single-cysteine mutant of Escherichia coli thioredoxin and

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11-17-2010, 11:15 PM

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

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

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

Eur J Biochem. 1998 Oct 15;257(2):299-308

Authors: Jeng MF, Reymond MT, Tennant LL, Holmgren A, Dyson HJ

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we have prepared a mutant of Escherichia coli thioredoxin where the second cysteine residue of the active site has been replaced by an alanine residue.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 residue and a short cysteine-containing peptide. This paper describes the preparation and characterization of the mutant protein both free and in the peptide complex.

PMID: 9826174 [PubMed - indexed for MEDLINE]

Source: PubMed

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