(14–38, 30–51) Double-disulphide intermediate in folding of bovine pancreatic trypsin inhibitor: A two-dimensional 1H nuclear magnetic resonance study
- 20 November 1991
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 222 (2) , 353-371
- https://doi.org/10.1016/0022-2836(91)90216-s
Abstract
No abstract availableKeywords
This publication has 49 references indexed in Scilit:
- Protein foldingBiochemical Journal, 1990
- [5]Disulfide bonds as probes of protein folding pathwaysPublished by Elsevier ,1986
- The problem of how and why proteins adopt folded conformationsThe Journal of Physical Chemistry, 1985
- Structure determination of a tetrasaccharide: transient nuclear Overhauser effects in the rotating frameJournal of the American Chemical Society, 1984
- Sequential resonance assignments in protein 1H nuclear magnetic resonance spectraJournal of Molecular Biology, 1982
- Accessibilities and reactivities of cysteine thiols during refolding of reduced bovine pancreatic trypsin inhibitorJournal of Molecular Biology, 1981
- Experimental studies of protein folding and unfoldingProgress in Biophysics and Molecular Biology, 1979
- Kinetics of refolding of reduced ribonucleaseJournal of Molecular Biology, 1977
- Conformational restrictions on the pathway of folding and unfolding of the pancreatic trypsin inhibitorJournal of Molecular Biology, 1977
- The two-disulphide intermediates and the folding pathway of reduced pancreatic trypsin inhibitorJournal of Molecular Biology, 1975