Disulfide bond-coupled folding of bovine pancreatic trypsin inhibitor derivatives missing one or two disulfide bonds

Biochemistry ◽  
1992 ◽  
Vol 31 (25) ◽  
pp. 5705-5717 ◽  
Author(s):  
Phyllis Anne Kosen ◽  
Cara B. Marks ◽  
Arnold M. Falick ◽  
Stephen Anderson ◽  
Irwin D. Kuntz
Keyword(s):  
Disulfide Bond ◽  
Trypsin Inhibitor ◽  
Disulfide Bonds ◽  
Bovine Pancreatic Trypsin Inhibitor ◽  
Pancreatic Trypsin Inhibitor

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

scholarly journals Genetic Selection for Enhanced Folding In Vivo Targets the Cys14-Cys38 Disulfide Bond in Bovine Pancreatic Trypsin Inhibitor

2011 ◽  
Vol 14 (6) ◽  
pp. 973-984 ◽  
Author(s):  
Linda Foit ◽  
Antje Mueller-Schickert ◽  
Bharath S. Mamathambika ◽  
Stefan Gleiter ◽  
Caitlyn L. Klaska ◽  
...  
Keyword(s):  
Disulfide Bond ◽  
Trypsin Inhibitor ◽  
Genetic Selection ◽  
Bovine Pancreatic Trypsin Inhibitor ◽  
Pancreatic Trypsin Inhibitor ◽  
Selection For

scholarly journals BPTI folding revisited: switching a disulfide into methylene thioacetal reveals a previously hidden path

2018 ◽  
Vol 9 (21) ◽  
pp. 4814-4820 ◽  
Author(s):  
Reem Mousa ◽  
Shifra Lansky ◽  
Gil Shoham ◽  
Norman Metanis
Keyword(s):  
Protein Structure ◽  
Protein Stability ◽  
Disulfide Bond ◽  
Trypsin Inhibitor ◽  
Biological Function ◽  
Bovine Pancreatic Trypsin Inhibitor ◽  
Folding Mechanism ◽  
Pancreatic Trypsin Inhibitor ◽  
Model Protein

The folding mechanism of the model protein bovine pancreatic trypsin inhibitor was revisited. By switching the solvent exposed disulfide bond with methylene thioacetal we uncovered a hidden pathway in its folding mechanism. In addition, this moiety enhanced protein stability while fully maintaining the protein structure and biological function.

Denaturant-dependent folding of bovine pancreatic trypsin inhibitor mutants with two intact disulfide bonds

Biochemistry ◽  
1990 ◽  
Vol 29 (18) ◽  
pp. 4410-4419 ◽  
Author(s):  
Mark R. Hurle ◽  
Cara B. Marks ◽  
Phyllis Anne Kosen ◽  
Stephen Anderson ◽  
Irwin D. Kuntz
Keyword(s):  
Trypsin Inhibitor ◽  
Disulfide Bonds ◽  
Bovine Pancreatic Trypsin Inhibitor ◽  
Pancreatic Trypsin Inhibitor

scholarly journals Crystal structure of an extensively simplified variant of bovine pancreatic trypsin inhibitor in which over one-third of the residues are alanines

2008 ◽  
Vol 105 (40) ◽  
pp. 15334-15339 ◽  
Author(s):  
Mohammad Monirul Islam ◽  
Shihori Sohya ◽  
Keiichi Noguchi ◽  
Masafumi Yohda ◽  
Yutaka Kuroda
Keyword(s):  
Trypsin Inhibitor ◽  
Disulfide Bonds ◽  
Accessible Surface Area ◽  
Chain Structure ◽  
Bovine Pancreatic Trypsin Inhibitor ◽  
Side Chain ◽  
Shape Complementarity ◽  
Pancreatic Trypsin Inhibitor ◽  
Folded Proteins ◽  
Hydrophobic Cores

We report the high-resolution crystal structures of an extensively simplified variant of bovine pancreatic trypsin inhibitor containing 20 alanines (BPTI-20st) and a reference single-disulfide-bonded variant (BPTI-[5,55]st) at, respectively, 1.39 and 1.09 Å resolutions. The sequence was simplified based on the results of an alanine scanning experiment, as reported previously. The effects of the multiple alanine substitutions on the overall backbone structure were surprisingly small (Cα atom RMSD of 0.53 Å) being limited to small local structural perturbations. Both BPTI variants retained a wild-type level of trypsin inhibitory activity. The side-chain configurations of residues buried in the hydrophobic cores (<30% accessible surface area) were almost perfectly retained in both BPTI-20st and BPTI-[5,55]st, indicating that neither multiple alanine replacements nor the removal of the disulfide bonds affected their precise placements. However, the side chains of three partially buried residues (Q31, R20, and to some extent Y21) and several unburied residues rearranged into alternative dense-packing structures, suggesting some plasticity in their shape complementarity. These results indicate that a protein sequence simplified over its entire length can retain its densely packed, native side-chain structure, and suggest that both the design and fold recognition of natively folded proteins may be easier than previously thought.

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