Distinct Folding Pathways of Two Homologous Disulfide Proteins: Bovine Pancreatic Trypsin Inhibitor and Tick Anticoagulant Peptide

2011 ◽  
Vol 14 (1) ◽  
pp. 127-135 ◽  
Author(s):  
Jui-Yoa Chang
Keyword(s):  
Trypsin Inhibitor ◽  
Bovine Pancreatic Trypsin Inhibitor ◽  
Folding Pathways ◽  
Pancreatic Trypsin Inhibitor ◽  
Tick Anticoagulant Peptide

scholarly journals Structure of tick anticoagulant peptide at 1.6 Å resolution complexed with bovine pancreatic trypsin inhibitor

2008 ◽  
Vol 9 (2) ◽  
pp. 265-272 ◽  
Author(s):  
Robert S. T. Charles ◽  
K. Padmanabhan ◽  
R. V. Arni ◽  
K. P. Padmanabhan ◽  
A. Tulinsky
Keyword(s):  
Trypsin Inhibitor ◽  
Bovine Pancreatic Trypsin Inhibitor ◽  
Pancreatic Trypsin Inhibitor ◽  
Tick Anticoagulant Peptide

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 Screening for Stable Mutants with Amino Acid Pairs Substituted for the Disulfide Bond between Residues 14 and 38 of Bovine Pancreatic Trypsin Inhibitor (BPTI)

2002 ◽  
Vol 277 (52) ◽  
pp. 51043-51048 ◽  
Author(s):  
Yoshihisa Hagihara ◽  
Kentaro Shiraki ◽  
Tsutomu Nakamura ◽  
Koichi Uegaki ◽  
Masahiro Takagi ◽  
...  
Keyword(s):  
Amino Acid ◽  
Disulfide Bond ◽  
Trypsin Inhibitor ◽  
Bovine Pancreatic Trypsin Inhibitor ◽  
Pancreatic Trypsin Inhibitor

Synthetic Approaches to Disulfide-free Circular Bovine Pancreatic Trypsin Inhibitor (c-BPTI) Analogues

2006 ◽  
Vol 12 (2) ◽  
pp. 93-104 ◽  
Author(s):  
Judit Tulla-Puche ◽  
Irina V. Getun ◽  
Yvonne M. Angell ◽  
Jordi Alsina ◽  
Fernando Albericio ◽  
...  
Keyword(s):  
Trypsin Inhibitor ◽  
Bovine Pancreatic Trypsin Inhibitor ◽  
Pancreatic Trypsin Inhibitor ◽  
Synthetic Approaches

A Pulsed-Field Gradient NMR Study of Bovine Pancreatic Trypsin Inhibitor Self-Association†

Biochemistry ◽  
1997 ◽  
Vol 36 (11) ◽  
pp. 3383-3388 ◽  
Author(s):  
Elena Ilyina ◽  
Vikram Roongta ◽  
Hong Pan ◽  
Clare Woodward ◽  
Kevin H. Mayo
Keyword(s):  
Field Gradient ◽  
Trypsin Inhibitor ◽  
Bovine Pancreatic Trypsin Inhibitor ◽  
Pulsed Field Gradient Nmr ◽  
Pulsed Field ◽  
Nmr Study ◽  
Pancreatic Trypsin Inhibitor ◽  
Self Association
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