Reexamination of the Folding of BPTI: Predominance of Native Intermediates
- 20 September 1991
- journal article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 253 (5026) , 1386-1393
- https://doi.org/10.1126/science.1716783
Abstract
Bovine pancreatic trypsin inhibitor (BPTI) continues to be the only protein for which a detailed pathway of folding has been described. Previous studies led to the conclusion that nonnative states are well populated in the oxidative folding of BPTI. This conclusion has broadly influenced efforts to understand protein folding. The population of intermediates present during the folding of BPTI has been reexamined by modern separation techniques. It was found that all well-populated folding intermediates contain only native disulfide bonds. These data emphasize the importance of native protein structure for understanding protein folding.Keywords
This publication has 43 references indexed in Scilit:
- The 5–55 single‐disulphide intermediate in folding of bovine pancreatic trypsin inhibitorFEBS Letters, 1991
- 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
- Detection of an early intermediate in the folding of ribonuclease A by protection of amide protons against exchangeJournal of Molecular Biology, 1979
- Hierarchic organization of domains in globular proteinsJournal of Molecular Biology, 1979
- Conformational restrictions on the pathway of folding and unfolding of the pancreatic trypsin inhibitorJournal of Molecular Biology, 1977
- Reactivities of the cysteine residues of the reduced pancreatic trypsin inhibitorJournal of Molecular Biology, 1975
- The single-disulphide intermediates in the refolding of reduced pancreatic trypsin inhibitorJournal of Molecular Biology, 1974
- 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