Kinetic roles and conformational properties of the non-native two-disulphide intermediates in the refolding of bovine pancreatic trypsin inhibitor
| Autor: | Thomas E. Creighton, Nigel J. Darby, G.H.E. Scott, David Neuhaus, C.P.M. van Mierlo |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 1992 |
| Předmět: |
Circular dichroism
Protein Denaturation Magnetic Resonance Spectroscopy Stereochemistry Protein Conformation Biochemie Biochemistry Aprotinin Structural Biology protein folding medicine Molecule Animals Disulfides Molecular Biology disulphide bonds chemistry.chemical_classification biology Circular Dichroism Protein engineering Trypsin Folding (chemistry) Kinetics bovine pancreatic trypsin inhibitor nuclear magnetic resonance Enzyme chemistry Enzyme inhibitor biology.protein Protein folding Cattle Electrophoresis Polyacrylamide Gel Spectrophotometry Ultraviolet medicine.drug |
| Zdroj: | Journal of Molecular Biology 224 (1992) Journal of Molecular Biology, 224, 905-911 |
| ISSN: | 0022-2836 |
| DOI: | 10.1016/0022-2836(92)90458-v |
| Popis: | The most productive folding pathway of reduced bovine pancreatic trypsin inhibitor (BPTI) proceeds through the disulphide intermediates (30–51), (30–51, 5–14), and (30–51, 5–38); these are important kinetic intermediates in folding, even though the latter pair contain non-native disulphide bonds. Analogues of these intermediates have been prepared by protein engineering methods and their conformational properties examined by circular dichroism and 1H-nuclear magnetic resonance. The (30–51), (30–51, 5–14) and (30–51, 5–38) analogues exhibit comparable degrees of stable structure, which cannot include those portions of the polypeptide chain involving Cys5, Cys14 and Cys38. These properties are consistent with the roles of (30–51, 5–14) and (30–51, 5–38) in the folding pathway of BPTI, which demand that they exhibit a considerable degree of conformational flexibility in part of the molecule. |
| Databáze: | OpenAIRE |
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