A new two-disulphide intermediate in the refolding of reduced bovine pancreatic trypsin inhibitor
- 5 April 1984
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 174 (2), 411-418
- https://doi.org/10.1016/0022-2836(84)90345-0
Abstract
No abstract availableKeywords
This publication has 22 references indexed in Scilit:
- A three-disulphide intermediate in refolding of reduced ribonuclease a with a folded conformationFEBS Letters, 1980
- Individual assignments of amide proton resonances in the proton NMR spectrum of the basic pancreatic trypsin inhibitorBiochimica et Biophysica Acta (BBA) - Protein Structure, 1979
- Experimental studies of protein folding and unfoldingProgress in Biophysics and Molecular Biology, 1979
- Immunochemical analysis of the conformational properties of intermediates trapped in the folding and unfolding of bovine pancreatic trypsin inhibitorJournal of Molecular Biology, 1978
- Two-dimensional spectroscopy. Application to nuclear magnetic resonanceThe Journal of Chemical Physics, 1976
- Interactions between cysteine residues as probes of protein conformation: The bisulphide bond between Cys-14 and Cys-38 of the pancreatic trypsin inhibitorJournal of Molecular Biology, 1975
- The two-disulphide intermediates and the folding pathway of reduced pancreatic trypsin inhibitorJournal of Molecular Biology, 1975
- Intermediates in the refolding of reduced pancreatic trypsin inhibitorJournal of Molecular Biology, 1974
- Renaturation of the reduced bovine pancreatic trypsin inhibitorJournal of Molecular Biology, 1974
- Location of disulphide bridges by diagonal paper electrophoresis. The disulphide bridges of bovine chymotrypsinogen A.Biochemical Journal, 1966