ArticleNano letters2019
Direction Matters: Monovalent Streptavidin/Biotin Complex under Load.
Article in Nano letters, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
26 citing papers in PubMed.
- Scalable production of monovalent streptavidin with high yield and purity.Scientific reports · 2026Article
- From Atoms to Cells: AI-Based Structure Prediction Fueling Molecular Dynamics Simulations in Computational Structural Biology.Advances in experimental medicine and biology · 2026Review
- UltrastrongScience advances · 2025Article
- Article
- The strongest protein binder is surprisingly labile.Protein science : a publication of the Protein Society · 2024Article
- Engineering the Mechanical Stability of a Therapeutic Affibody/PD-L1 Complex by Anchor Point Selection.bioRxiv : the preprint server for biology · 2024Article
- Engineering an artificial catch bond using mechanical anisotropy.Nature communications · 2024Article
- Fostering discoveries in the era of exascale computing: How the next generation of supercomputers empowers computational and experimental biophysics alike.Biophysical journal · 2023Review
- Anisotropic Friction in a Ligand-Protein Complex.Nano letters · 2023Article
- Sortase A transpeptidation produces seamless, unbranched biotinylated nanobodies for multivalent and multifunctional applications.Nanoscale advances · 2023Article
- Interaction of theACS nanoscience Au · 2023Article
- May the force be with you: The role of hyper-mechanostability of the bone sialoprotein binding protein during early stages ofFrontiers in chemistry · 2023Article
- Acoustic force spectroscopy reveals subtle differences in cellulose unbinding behavior of carbohydrate-binding modules.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Mechanical Stabilization of a Bacterial Adhesion Complex.Journal of the American Chemical Society · 2022Article
- Optical Fluorescence Imaging of Native Proteins Using a Fluorescent Probe with a Cell-Membrane-Permeable Carboxyl Group.International journal of molecular sciences · 2022Article
- Correlating single-molecule rupture mechanics with cell population adhesion by yeast display.Biophysical reports · 2022Article
- Mapping Mechanostable Pulling Geometries of a Therapeutic Anticalin/CTLA-4 Protein Complex.Nano letters · 2022Article
- Tethering Complex Proteins and Protein Complexes for Optical Tweezers Experiments.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Protein structure prediction in the era of AI: Challenges and limitations when applying toFrontiers in bioinformatics · 2022Article
- Model systems for optical trapping: the physical basis and biological applications.Biophysical reviews · 2021Review
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
Novel site-specific attachment strategies combined with improvements of computational resources enable new insights into the mechanics of the monovalent biotin/streptavidin complex under load and forced us to rethink the diversity of rupture forces reported in the literature. We discovered that the mechanical stability of this complex depends strongly on the geometry in which force is applied. By atomic force microscopy-based single molecule force spectroscopy we found unbinding of biotin to occur beyond 400 pN at force loading rates of 10 nN/s when monovalent streptavidin was tethered at its C-terminus. This value is about twice as high than that for N-terminal attachment. Steered molecular dynamics simulations provided a detailed picture of the mechanics of the unbinding process in the corresponding force loading geometries. Using machine learning techniques, we connected findings from hundreds of simulations to the experimental results, identifying different force propagation pathways. Interestingly, we observed that depending on force loading geometry, partial unfolding of N-terminal region of monovalent streptavidin occurs before biotin is released from the binding pocket.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.