ArticleThe Journal of biological chemistry2017
The influence of disulfide bonds on the mechanical stability of proteins is context dependent.
Article in The Journal of biological chemistry, 2017. 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, 54 citations in OpenAlex.
- The Impact of Purified Granules Sourced from Potato, Maize and Wheat on Disulfide Bond Formation in Urea-Solubilized Glutenin.Foods (Basel, Switzerland) · 2026Article
- Investigating the structural basis of surfactant protein D oligomerization: The crucial role of Cys15-Cys15/Cys20-Cys20 disulfide bond linkage.Protein science : a publication of the Protein Society · 2026Article
- Chemical and photoinduced interstrand crosslinking of oligo DNA duplexes containing 2'-deoxythioguanosines.Communications chemistry · 2025Article
- Comparative genomic analysis of thermophilic fungi reveals convergent evolutionary adaptations and gene losses.Communications biology · 2024Article
- Article
- Enterocin DD14 can inhibit the infection of eukaryotic cells with enveloped viruses.Archives of microbiology · 2024Article
- Engineered ice-binding protein (FfIBP) shows increased stability and resistance to thermal and chemical denaturation compared to the wildtype.Scientific reports · 2024Article
- Co-translational formation of disulfides guides folding of the SARS-CoV-2 receptor binding domain.Biophysical journal · 2023Article
- Alterations of bovine nucleus pulposus cells with aging.Aging cell · 2023Article
- Native and Engineered Cyclic Disulfide-Rich Peptides as Drug Leads.Molecules (Basel, Switzerland) · 2023Review
- Specific chiroptical sensing of cysteine via ultrasound-assisted formation of disulfide bonds in aqueous solution.Ultrasonics sonochemistry · 2022Article
- Protein nanomechanics in biological context.Biophysical reviews · 2021Review
- 3D interaction homology: Hydropathic interaction environments of serine and cysteine are strikingly different and their roles adapt in membrane proteins.Current research in structural biology · 2021Article
- Regulation of titin-based cardiac stiffness by unfolded domain oxidation (UnDOx).Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Next Generation Methods for Single-Molecule Force Spectroscopy on Polyproteins and Receptor-Ligand Complexes.Frontiers in molecular biosciences · 2020Review
- Removal of a Conserved Disulfide Bond Does Not Compromise Mechanical Stability of a VHH Antibody Complex.Nano letters · 2019Article
- Redox regulation of protein nanomechanics in health and disease: Lessons from titin.Redox biology · 2019Review
- n→π* Interactions Modulate the Properties of Cysteine Residues and Disulfide Bonds in Proteins.Journal of the American Chemical Society · 2018Article
- Mechanical architecture and folding of E. coli type 1 pilus domains.Nature communications · 2018Article
- Disulfide isomerization reactions in titin immunoglobulin domains enable a mode of protein elasticity.Nature communications · 2018Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Disulfide bonds play a crucial role in proteins, modulating their stability and constraining their conformational dynamics. A particularly important case is that of proteins that need to withstand forces arising from their normal biological function and that are often disulfide bonded. However, the influence of disulfides on the overall mechanical stability of proteins is poorly understood. Here, we used single-molecule force spectroscopy (smFS) to study the role of disulfide bonds in different mechanical proteins in terms of their unfolding forces. For this purpose, we chose the pilus protein FimG from Gram-negative bacteria and a disulfide-bonded variant of the I91 human cardiac titin polyprotein. Our results show that disulfide bonds can alter the mechanical stability of proteins in different ways depending on the properties of the system. Specifically, disulfide-bonded FimG undergoes a 30% increase in its mechanical stability compared with its reduced counterpart, whereas the unfolding force of I91 domains experiences a decrease of 15% relative to the WT form. Using a coarse-grained simulation model, we rationalized that the increase in mechanical stability of FimG is due to a shift in the mechanical unfolding pathway. The simple topology-based explanation suggests a neutral effect in the case of titin. In summary, our results indicate that disulfide bonds in proteins act in a context-dependent manner rather than simply as mechanical lockers, underscoring the importance of considering disulfide bonds both computationally and experimentally when studying the mechanical properties of proteins.
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