ArticleNature communications2018
Calcium stabilizes the strongest protein fold.
Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- UltrastrongScience advances · 2025Article
- Real-time genome imaging of host interactions in adeno-associated virus genome release.iScience · 2025Article
- Mechanochemistry: Fundamental Principles and Applications.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Review
- Mechanical forces and ligand binding modulateLife science alliance · 2025Article
- Computational insights into DC-SIGN's enhanced recognition of mannotriose CPS units via CaGlycoconjugate journal · 2025Article
- The strongest protein binder is surprisingly labile.Protein science : a publication of the Protein Society · 2024Article
- Optimizing Bothropstoxin-I-Derived Peptides: Exploring the Antibacterial Potential of p-BthW.ACS omega · 2024Article
- Fermentation Practices Select for Thermostable Endolysins in Phages.Molecular biology and evolution · 2024Article
- The Ruminococcus bromii amylosome protein Sas6 binds single and double helical α-glucan structures in starch.Nature structural & molecular biology · 2024Article
- Characterization of a New Glucose-Tolerant GH1 β-Glycosidase fromInternational journal of molecular sciences · 2023Article
- New insights into the folding-unfolding mechanism and conformations of cytochrome C.Chemical science · 2022Article
- Optimal Sacrificial Domains in Mechanical Polyproteins:JACS Au · 2022Article
- Mycobacterial Adhesion: From Hydrophobic to Receptor-Ligand Interactions.Microorganisms · 2022Review
- Strategies to prevent, curb and eliminate biofilm formation based on the characteristics of various periods in one biofilm life cycle.Frontiers in cellular and infection microbiology · 2022Review
- The biophysics of bacterial infections: Adhesion events in the light of force spectroscopy.Cell surface (Amsterdam, Netherlands) · 2021Article
- An ester bond underlies the mechanical strength of a pathogen surface protein.Nature communications · 2021Article
- Protein nanomechanics in biological context.Biophysical reviews · 2021Review
- Mechanical Stability of a Small, Highly-Luminescent Engineered Protein NanoLuc.International journal of molecular sciences · 2020Article
- Protein Homeostasis Networks and the Use of Yeast to Guide Interventions in Alzheimer's Disease.International journal of molecular sciences · 2020Review
- Mechanisms of Nanonewton Mechanostability in a Protein Complex Revealed by Molecular Dynamics Simulations and Single-Molecule Force Spectroscopy.Journal of the American Chemical Society · 2019Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Staphylococcal pathogens adhere to their human targets with exceptional resilience to mechanical stress, some propagating force to the bacterium via small, Ig-like folds called B domains. We examine the mechanical stability of these folds using atomic force microscopy-based single-molecule force spectroscopy. The force required to unfold a single B domain is larger than 2 nN - the highest mechanostability of a protein to date by a large margin. B domains coordinate three calcium ions, which we identify as crucial for their extreme mechanical strength. When calcium is removed through chelation, unfolding forces drop by a factor of four. Through systematic mutations in the calcium coordination sites we can tune the unfolding forces from over 2 nN to 0.15 nN, and dissect the contribution of each ion to B domain mechanostability. Their extraordinary strength, rapid refolding and calcium-tunable force response make B domains interesting protein design targets.
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