Prediction of protein folding pathways: Bovine pancreatic trypsin inhibitor

1993 ◽  
Vol 11 (S1) ◽  
pp. S67-S71 ◽  
Author(s):  
G. Chelvanayagam ◽  
P. Argos
Keyword(s):  
Protein Folding ◽  
Trypsin Inhibitor ◽  
Bovine Pancreatic Trypsin Inhibitor ◽  
Folding Pathways ◽  
Pancreatic Trypsin Inhibitor ◽  
Protein Folding Pathways

Disulphide-coupled protein folding pathways

1995 ◽  
Vol 348 (1323) ◽  
pp. 5-10 ◽  
Keyword(s):  
Protein Folding ◽  
Trypsin Inhibitor ◽  
Native Species ◽  
Molten Globule ◽  
Disulphide Bond ◽  
Bovine Pancreatic Trypsin Inhibitor ◽  
Disulphide Bond Formation ◽  
Folding Pathways ◽  
Pancreatic Trypsin Inhibitor ◽  
Protein Folding Pathways

Protein folding pathways that involve disulphide bond formation can be determined in great detail. Those of bovine pancreatic trypsin inhibitor, α-lactalbumin and ribonucleases A and T 1 are compared and contrasted. In each species, whatever conformation favours one disulphide bond over another is stabilized to the same extent by the presence of that disulphide bond in the disulphide intermediates. The pathways differ markedly in the nature of that conformation: in bovine pancreatic trypsin inhibitor a crucial intermediate is partly folded, in α-lactalbumin the intermediates tend to adopt to varying extents the molten globule conformation, while in the ribonucleases the early disulphide intermediates are largely unfolded, and none predominate. In each case, however, the slowest step is formation of a disulphide bond that will be buried in a stable folded conformation; the most rapid step is formation of an accessible disulphide bond on the surface of a folded conformation. Quasi-native species with the native conformation, but incomplete disulphide bonds, can either increase or decrease the rate of further disulphide formation.

scholarly journals Disulfide bonds in protein folding studies: friends or foes?

1997 ◽  
Vol 44 (3) ◽  
pp. 433-452 ◽  
Author(s):  
M Dadlez
Keyword(s):  
Protein Folding ◽  
Disulfide Bonds ◽  
Model Systems ◽  
Bovine Pancreatic Trypsin Inhibitor ◽  
General Mechanism ◽  
Folding Pathway ◽  
Protein Model ◽  
Folding Pathways ◽  
Pancreatic Trypsin Inhibitor ◽  
Protein Folding Pathways

The studies on protein folding pathways utilizing disulfide bonds as reporter groups in several protein model systems are reviewed. Implications for a general mechanism of protein folding are discussed. An updated folding pathway for bovine pancreatic trypsin inhibitor (BPTI) based on recent data is proposed.

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