Distribution of Disulfide Bonds in the Two-Disulfide Intermediates in the Regeneration of Bovine Pancreatic Ribonuclease A: Further Insights into the Folding Process
Author:
Affiliation:
1. Baker Laboratory of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14853-1301
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi990570f
Reference39 articles.
1. Regeneration of Bovine Pancreatic Ribonuclease A: Identification of Two Nativelike Three-Disulfide Intermediates Involved in Separate Pathways
2. Regeneration of Bovine Pancreatic Ribonuclease A: Detailed Kinetic Analysis of Two Independent Folding Pathways
3. An Unusual Adduct of Dithiothreitol with a Pair of Cysteine Residues of a Protein as a Stable Folding Intermediate
4. Kinetic Folding Pathway of a Three-Disulfide Mutant of Bovine Pancreatic Ribonuclease A Missing the [40−95] Disulfide Bond
5. 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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1. The Non-native Disulfide-Bond-Containing Landscape Orthogonal to the Oxidative Protein-Folding Trajectory: A Necessary Evil?;The Journal of Physical Chemistry B;2022-12-06
2. Mechanical Stability of Ribonuclease A Heavily Depends on the Redox Environment;The Journal of Physical Chemistry B;2022-08-17
3. Securing Native Disulfide Bonds in Disulfide-Coupled Protein Folding Reactions: The Role of Intrinsic and Extrinsic Elements vis-à-vis Protein Aggregation and Neurodegeneration;ACS Omega;2021-11-16
4. The Formation of Native Disulfide Bonds: Treading a Fine Line in Protein Folding;The Protein Journal;2021-03-25
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