ArticleScientific reports2017
Accessibility explains preferred thiol-disulfide isomerization in a protein domain.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- Post-Translational Modifications to Cysteine Residues in Plant Proteins and Their Impact on the Regulation of Metabolism and Signal Transduction.International journal of molecular sciences · 2024Review
- Vitamin K Epoxide Reductase Complex-Protein Disulphide Isomerase Assemblies in the Thiol-Disulphide Exchange Reactions: Portrayal of Precursor-to-Successor Complexes.International journal of molecular sciences · 2024Article
- Label-free biomolecular and cellular methods in small molecule epigallocatechin-gallate research.Heliyon · 2024Review
- Synergy of Mutation-Induced Effects in Human Vitamin K Epoxide Reductase: Perspectives and Challenges for Allo-Network Modulator Design.International journal of molecular sciences · 2024Article
- Co-translational formation of disulfides guides folding of the SARS-CoV-2 receptor binding domain.Biophysical journal · 2023Article
- Novel carbon nanozymes with enhanced phosphatase-like catalytic activity for antimicrobial applications.Discover nano · 2023Article
- Real-time imaging of sulfhydryl single-stranded DNA aggregation.Communications chemistry · 2023Article
- Impact of SARS-CoV-2 RBD Mutations on the Production of a Recombinant RBD Fusion Protein in Mammalian Cells.Biomolecules · 2022Article
- Human Vitamin K Epoxide Reductase as a Target of Its Redox Protein.International journal of molecular sciences · 2022Article
- Catch, Modify and Analyze: Methods of Chemoselective Modification of Cysteine-Containing Peptides.Molecules (Basel, Switzerland) · 2022Review
- A proximity-based in silico approach to identify redox-labile disulfide bonds: The example of FVIII.PloS one · 2022Article
- Thioredoxin Dependent Changes in the Redox States of FurA fromAntioxidants (Basel, Switzerland) · 2021Article
- A clickable probe for versatile characterization of S-nitrosothiols.Redox biology · 2020Article
- ADAM17 cytoplasmic domain modulates Thioredoxin-1 conformation and activity.Redox biology · 2020Article
- Mechanisms of Disulfide Bond Formation in Nascent Polypeptides Entering the Secretory Pathway.Cells · 2020Review
- Article
- Molecular basis for potentiation of Cx36 gap junction channel conductance byBioscience reports · 2018Article
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3 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Disulfide bonds are key stabilizing and yet potentially labile cross-links in proteins. While spontaneous disulfide rearrangement through thiol-disulfide exchange is increasingly recognized to play an important physiological role, its molecular determinants are still largely unknown. Here, we used a novel hybrid Monte Carlo and Molecular Dynamics scheme to elucidate the molecular principles of thiol-disulfide exchange in proteins, for a mutated immunoglobulin domain as a model system. Unexpectedly, using simple proximity as the criterion for thiol-disulfide exchange, our method correctly predicts the experimentally observed regiospecificity and selectivity of the cysteine-rich protein. While redox reactivity has been examined primarily on the level of transition states and activation barriers, our results argue for accessibility of the disulfide by the attacking thiol given the highly dynamic and sterically demanding protein as a major bottleneck of thiol-disulfide exchange. This scenario may be similarly at play in other proteins with or without an evolutionarily designed active site.
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