Random circular permutation of DsbA reveals segments that are essential for protein folding and stability
- 5 March 1999
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 286 (4), 1197-1215
- https://doi.org/10.1006/jmbi.1998.2531
Abstract
No abstract availableKeywords
This publication has 70 references indexed in Scilit:
- Reconstitution of a Protein Disulfide Catalytic SystemPublished by Elsevier ,1998
- Active barnase variants with completely random hydrophobic cores.Proceedings of the National Academy of Sciences, 1996
- The nature of protein folding pathways: The classical versus the new viewJournal of Biomolecular NMR, 1995
- Mutants in disulfide bond formation that disrupt flagellar assembly in Escherichia coli.Proceedings of the National Academy of Sciences, 1993
- Identification of a protein required for disulfide bond formation in vivoCell, 1991
- A genetic screen to identify variants of bovine pancreatic trypsin inhibitor with altered folding energeticsProteins-Structure Function and Bioinformatics, 1990
- Temperature-sensitive mutations of bacteriophage T4 lysozyme occur at sites with low mobility and low solvent accessibility in the folded proteinBiochemistry, 1987
- The Complete Covalent Structure of Hirudin. Localization of the Disulfide BondsBiological Chemistry Hoppe-Seyler, 1985
- Principles that Govern the Folding of Protein ChainsScience, 1973
- Tissue sulfhydryl groupsArchives of Biochemistry and Biophysics, 1959