Folding of a disulfide-bonded protein species with free thiol(s): competition between conformational folding and disulfide reshuffling in an intermediate of bovine pancreatic ribonuclease A.

No abstract is available for this paper.

• Publication year

  2001

• Venue

  Biochemistry

• Publication date

  2001-12-11

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1021/BI010781WPMID 11732921
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• Structural determinants of oxidative folding in proteins

  2001cited by this paper
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  2001cited by this paper
• Coupling of conformational folding and disulfide-bond reactions in oxidative folding of proteins.

  2001cited by this paper
• Oxidative folding of proteins.

  2000cited by this paper
• Disulfide bonds and protein folding.

  2000cited by this paper
• Contribution of disulfide bonds to the conformational stability and catalytic activity of ribonuclease A.

  2000cited by this paper
• Conformational unfolding studies of three-disulfide mutants of bovine pancreatic ribonuclease A and the coupling of proline isomerization to disulfide redox reactions.

  1999cited by this paper
• Two new structured intermediates in the oxidative folding of RNase A

  1999cited by this paper
• Comparison of local and global stability of an analogue of a disulfide-folding intermediate with those of the wild-type protein in bovine pancreatic ribonuclease A: identification of specific regions of stable structure along the oxidative folding pathway.

  1999cited by this paper
• Regeneration of bovine pancreatic ribonuclease A: detailed kinetic analysis of two independent folding pathways.

  1998cited by this paper
• The burst phase in ribonuclease A folding and solvent dependence of the unfolded state

  1998cited by this paper
• Regeneration of three-disulfide mutants of bovine pancreatic ribonuclease A missing the 65-72 disulfide bond: characterization of a minor folding pathway of ribonuclease A and kinetic roles of Cys65 and Cys72.

  1998cited by this paper
• Kinetic folding pathway of a three-disulfide mutant of bovine pancreatic ribonuclease A missing the [40-95] disulfide bond.

  1998cited by this paper
• Crystal structures of two mutants that have implications for the folding of bovine pancreatic ribonuclease A

  1998cited by this paper
• Regeneration of bovine pancreatic ribonuclease A: identification of two nativelike three-disulfide intermediates involved in separate pathways.

  1998cited by this paper
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  1997cited by this paper
• Protein Disulfide Isomerase and Assisted Protein Folding*

  1997cited by this paper
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  1997cited by this paper
• Structural characterization of an analog of the major rate-determining disulfide folding intermediate of bovine pancreatic ribonuclease A.

  1997cited by this paper
• Folding studies on ribonuclease A, a model protein.

  1997cited by this paper
• Tyrosyl interactions in the folding and unfolding of bovine pancreatic ribonuclease A: a study of tyrosine-to-phenylalanine mutants.

  1997cited by this paper
• Mechanism of reductive protein unfolding

  1995cited by this paper
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  1994cited by this paper
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  1994cited by this paper
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  1993cited by this paper
• Expression of wild-type and mutant bovine pancreatic ribonuclease A in Escherichia coli.

  1993cited by this paper
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  1992cited by this paper
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  1990cited by this paper
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  1988cited by this paper
• Catalysis of proline isomerization during protein-folding reactions.

  1988cited by this paper
• Disulphide bridges in globular proteins.

  1981cited by this paper
• Both the fast and slow refolding reactions of ribonuclease A yield native enzyme.

  1973cited by this paper
• Structural studies of pancreatic ribonuclease.

  1967cited by this paper

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