Screening for stable mutants with amino acid pairs substituted for the disulfide bond between residues 14 and 38 of bovine pancreatic trypsin inhibitor (BPTI). (Q30865816)

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English	Screening for stable mutants with amino acid pairs substituted for the disulfide bond between residues 14 and 38 of bovine pancreatic trypsin inhibitor (BPTI).	scientific article

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14 December 2019

Screening for stable mutants with amino acid pairs substituted for the disulfide bond between residues 14 and 38 of bovine pancreatic trypsin inhibitor (BPTI) (English)

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14 December 2019

Yoshihisa Hagihara

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14 December 2019

Tsutomu Nakamura

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14 December 2019

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Kentaro Shiraki

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14 December 2019

Koichi Uegaki

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14 December 2019

Masahiro Takagi

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14 December 2019

Tadayuki Imanaka

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14 December 2019

Noboru Yumoto

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21 October 2002

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14 December 2019

Journal of Biological Chemistry

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14 December 2019

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14 December 2019

51043-51048

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14 December 2019

Complete folding of bovine pancreatic trypsin inhibitor with only a single disulfide bond

1 reference

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Disulfide bond effects on protein stability: designed variants of Cucurbita maxima trypsin inhibitor-V.

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The Role of the Intrachain Disulfide Bond in the Conformation and Stability of the Constant Fragment of the Immunoglobulin Light Chain1

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Protein folding stability can determine the efficiency of escape from endoplasmic reticulum quality control

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Secretion efficiency in Saccharomyces cerevisiae of bovine pancreatic trypsin inhibitor mutants lacking disulfide bonds is correlated with thermodynamic stability

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Folding of bovine pancreatic trypsin inhibitor (BPTI) variants in which almost half the residues are alanine.

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"Designing out" disulfide bonds: thermodynamic properties of 30-51 cystine substitution mutants of bovine pancreatic trypsin inhibitor.

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Contribution of individual side-chains to the stability of BPTI examined by alanine-scanning mutagenesis

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Spectroscopic Determination of Tryptophan and Tyrosine in Proteins*

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Alanine point-mutations in the reactive region of bovine pancreatic trypsin inhibitor: effects on the kinetics and thermodynamics of binding to beta-trypsin and alpha-chymotrypsin.

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21 January 2018

Thermodynamics of BPTI folding

1 reference

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Protein aggregation: folding aggregates, inclusion bodies and amyloid

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Removal of the conserved disulfide bridges from the scfv fragment of an antibody: effects on folding kinetics and aggregation

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Antibody scFv fragments without disulfide bonds made by molecular evolution

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A kinetic explanation for the rearrangement pathway of BPTI folding

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Basic pancreatic trypsin inhibitor has unusual thermodynamic stability parameters

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21 January 2018

Stability studies on derivatives of the bovine pancreatic trypsin inhibitor

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

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Enthalpic destabilization of a mutant human lysozyme lacking a disulfide bridge between cysteine-77 and cysteine-95

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Identifiers

10.1074/JBC.M208893200

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Europe PubMed Central

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14 December 2019

1 reference

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14 December 2019

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