Comparative analysis of the active-site 3D structures of thiol-protein oxidoreductases and related synthetic fragments
- 1 January 1995
- book chapter
- Published by Springer Nature
Abstract
No abstract availableThis publication has 6 references indexed in Scilit:
- Protein disulphide isomerase: building bridges in protein foldingTrends in Biochemical Sciences, 1994
- Structure-dependent redox potentials of active-site fragments of thiol protein oxidoreductasesPublished by Springer Nature ,1994
- The Redox Properties of Protein Disulfide Isomerase (DsbA) of Escherichia coli Result from a Tense Conformation of its Oxidized FormJournal of Molecular Biology, 1993
- Crystal structure of the DsbA protein required for disulphide bond formation in vivoNature, 1993
- Redox potentials of active-site bis(cysteinyl) fragments of thiol-protein oxidoreductasesBiochemistry, 1993
- Energetic and structural basis for the preferential formation of the native disulfide loop involving Cys-65 and Cys-72 in synthetic peptide fragments derived from the sequence of ribonuclease AJournal of the American Chemical Society, 1993