Bovine pancreatic ribonuclease A: oxidative and conformational folding studies.

No abstract is available for this paper.

• Publication year

  2001

• Venue

  Methods in Enzymology

• Publication date

  Unknown publication date

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1016/S0076-6879(01)41153-0PMID 11582778
• 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.

• Solution NMR evidence for a cis Tyr‐Ala peptide group in the structure of [Pro93Ala] bovine pancreatic ribonuclease A

  2008cited by this paper
• Local and long-range interactions in the thermal unfolding transition of bovine pancreatic ribonuclease A.

  2001cited by this paper
• Mechanisms of protein folding.

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• Structural determinants of oxidative folding in proteins

  2001cited by this paper
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• Disulfide bonds and protein folding.

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• Contribution of disulfide bonds to the conformational stability and catalytic activity of ribonuclease A.

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• Oxidative folding of proteins.

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• Acceleration of oxidative folding of bovine pancreatic ribonuclease A by anion‐induced stabilization and formation of structured native‐like intermediates

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• 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.

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• Structural characterization of an analog of the major rate-determining disulfide folding intermediate of bovine pancreatic ribonuclease A.

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• Reduced‐denatured ribonuclease A is not in a compact state

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• Thermal unfolding and proteolytic susceptibility of ribonuclease A.

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• Ionic interactions in crystalline bovine pancreatic ribonuclease A.

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• Characterization of the pH titration shifts of ribonuclease A by one- and two-dimensional nuclear magnetic resonance spectroscopy.

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  1994cited by this paper
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