ArticleBiophysical journal2014
Identification of allosteric disulfides from prestress analysis.
Article in Biophysical journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- Article
- Estimate of Numbers of Disulfide-Bonded Protein States.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Classification of Protein Disulfide Bonds.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Structural and functional insights into acidophilic helicases as DNA-unwinding motors.Applied and environmental microbiology · 2025Article
- Patient anti-FVIII drug antibodies bind preferentially to a subset of FVIII covalent states.Blood advances · 2025Article
- Article
- ARIP: A Tool for Precise Interatomic Contact Area and Volume Calculation in Proteins.International journal of molecular sciences · 2024Article
- Article
- Article
- Quantification of von Willebrand factor and ADAMTS-13 after traumatic injury: a pilot study.Trauma surgery & acute care open · 2021Article
- Multiple Disulfide-Bonded States of Native Proteins: Estimate of Number Using Probabilities of Disulfide Bond Formation.Molecules (Basel, Switzerland) · 2020Article
- Local frustration determines loop opening during the catalytic cycle of an oxidoreductase.eLife · 2020Article
- Allosteric disulphide bonds as reversible mechano-sensitive switches that control protein functions in the vasculature.Biophysical reviews · 2019Review
- Cys.sqlite: A Structured-Information Approach to the Comprehensive Analysis of Cysteine Disulfide Bonds in the Protein Databank.Journal of chemical information and modeling · 2019Article
- Allosteric disulfides: Sophisticated molecular structures enabling flexible protein regulation.The Journal of biological chemistry · 2019Review
- Mechano-redox control of integrin de-adhesion.eLife · 2018Article
- Identification of allosteric disulfides from labile bonds in X-ray structures.Royal Society open science · 2018Article
- The influence of disulfide bonds on the mechanical stability of proteins is context dependent.The Journal of biological chemistry · 2017Article
- From structure to redox: The diverse functional roles of disulfides and implications in disease.Proteomics · 2017Review
- One-Way Allosteric Communication between the Two Disulfide Bonds in Tissue Factor.Biophysical journal · 2017Article
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Disulfide bonds serve to form physical cross-links between residues in protein structures, thereby stabilizing the protein fold. Apart from this purely structural role, they can also be chemically active, participating in redox reactions, and they may even potentially act as allosteric switches controlling protein functions. Specific types of disulfide bonds have been identified in static protein structures from their distinctive pattern of dihedral bond angles, and the allosteric function of such bonds is purported to be related to the torsional strain they store. Using all-atom molecular-dynamics simulations for ∼700 disulfide bonded proteins, we analyzed the intramolecular mechanical forces in 20 classes of disulfide bonds. We found that two particular classes, the -RHStaple and the -/+RHHook disulfides, are indeed more stressed than other disulfide bonds, but the stress is carried primarily by stretching of the S-S bond and bending of the neighboring bond angles, rather than by dihedral torsion. This stress corresponds to a tension force of magnitude ∼200 pN, which is balanced by repulsive van der Waals interactions between the cysteine Cα atoms. We confirm stretching of the S-S bond to be a general feature of the -RHStaples and the -/+RHHooks by analyzing ∼20,000 static protein structures. Given that forced stretching of S-S bonds is known to accelerate their cleavage, we propose that prestress of allosteric disulfide bonds has the potential to alter the reactivity of a disulfide, thereby allowing us to readily switch between functional states.
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