Native and non-native intermediates in the BPTI folding pathway
- 1 July 1992
- journal article
- review article
- Published by Elsevier in Trends in Biochemical Sciences
- Vol. 17 (7) , 257-261
- https://doi.org/10.1016/0968-0004(92)90405-x
Abstract
No abstract availableKeywords
This publication has 16 references indexed in Scilit:
- Kinetic roles and conformational properties of the non-native two-disulphide intermediates in the refolding of bovine pancreatic trypsin inhibitorJournal of Molecular Biology, 1992
- Two-dimensional 1H nuclear magnetic resonance study of the (5–55) single-disulphide folding intermediate of bovine pancreatic trypsin inhibitorJournal of Molecular Biology, 1991
- (14–38, 30–51) Double-disulphide intermediate in folding of bovine pancreatic trypsin inhibitor: A two-dimensional 1H nuclear magnetic resonance studyJournal of Molecular Biology, 1991
- Reexamination of the Folding of BPTI: Predominance of Native IntermediatesScience, 1991
- The 5–55 single‐disulphide intermediate in folding of bovine pancreatic trypsin inhibitorFEBS Letters, 1991
- Mutational analysis of a protein-folding pathwayNature, 1989
- A peptide model of a protein folding intermediateNature, 1988
- Conformations of intermediates in the folding of the pancreatic trypsin inhibitorJournal of Molecular Biology, 1987
- Kinetic role of a meta-stable native-like two-disulphide species in the folding transition of bovine pancreatic trypsin inhibitorJournal of Molecular Biology, 1984
- A new two-disulphide intermediate in the refolding of reduced bovine pancreatic trypsin inhibitorJournal of Molecular Biology, 1984