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NMR characterization of a single-cysteine mutant of Escherichia coli thioredoxin and a covalent thioredoxin-peptide complex.
- Source :
- European Journal of Biochemistry; Oct98 Part 2, Vol. 257 Issue 2, p299-308, 10p, 2 Diagrams, 2 Charts, 5 Graphs
- Publication Year :
- 1998
-
Abstract
- 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we have prepared a mutant of Escherichia coli thioredoxin where the second cysteine residue of the active site has been replaced by an alanine residue.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. [ABSTRACT FROM AUTHOR]
- Subjects :
- THIOREDOXIN
ESCHERICHIA coli
NUCLEAR magnetic resonance
Subjects
Details
- Language :
- English
- ISSN :
- 00142956
- Volume :
- 257
- Issue :
- 2
- Database :
- Complementary Index
- Journal :
- European Journal of Biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 5276943
- Full Text :
- https://doi.org/10.1046/j.1432-1327.1998.2570299.x