Secretion Efficiency inSaccharomyces cerevisiaeof Bovine Pancreatic Trypsin Inhibitor Mutants Lacking Disulfide Bonds Is Correlated with Thermodynamic Stability†

Biochemistry ◽  
1998 ◽  
Vol 37 (5) ◽  
pp. 1264-1273 ◽  
Author(s):  
Jean M. Kowalski ◽  
Rajesh N. Parekh ◽  
K. Dane Wittrup
Keyword(s):  
Trypsin Inhibitor ◽  
Thermodynamic Stability ◽  
Disulfide Bonds ◽  
Bovine Pancreatic Trypsin Inhibitor ◽  
Pancreatic Trypsin Inhibitor ◽  
Secretion Efficiency

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

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.

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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