ArticleBiophysical journal2016
Kinetic Ductility and Force-Spike Resistance of Proteins from Single-Molecule Force Spectroscopy.
Article in Biophysical journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Single-Molecule Force Spectroscopy: Experiments, Analysis, and Simulations.Methods in molecular biology (Clifton, N.J.) · 2027Article
- A theoretical framework for random acceleration molecular dynamics simulations.The Journal of chemical physics · 2026Article
- Modulation of SARS-CoV-2 spike binding to ACE2 through conformational selection.Nature nanotechnology · 2025Article
- On the distance to the transition state of protein folding in optical tweezers experiments.Biophysical reviews · 2025Review
- From viral assembly to host interaction: AFM's contributions to virology.Journal of virology · 2025Review
- Good Rates From Bad Coordinates: The Exponential Average Time-dependent Rate Approach.Journal of chemical theory and computation · 2024Article
- Microscopic theory, analysis, and interpretation of conductance histograms in molecular junctions.Nature communications · 2023Article
- Biological physics by high-speed atomic force microscopy.Philosophical transactions. Series A, Mathematical, physical, and engineering sciences · 2020Review
- The SecA motor generates mechanical force during protein translocation.Nature communications · 2020Article
- High-speed force spectroscopy: microsecond force measurements using ultrashort cantilevers.Biophysical reviews · 2019Review
- Heterogeneous and rate-dependent streptavidin-biotin unbinding revealed by high-speed force spectroscopy and atomistic simulations.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Structural-elastic determination of the force-dependent transition rate of biomolecules.Chemical science · 2018Article
- Forced-rupture of cell-adhesion complexes reveals abrupt switch between two brittle states.The Journal of chemical physics · 2018Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Ductile materials can absorb spikes in mechanical force, whereas brittle ones fail catastrophically. Here we develop a theory to quantify the kinetic ductility of single molecules from force spectroscopy experiments, relating force-spike resistance to the differential responses of the intact protein and the unfolding transition state to an applied mechanical force. We introduce a class of unistable one-dimensional potential surfaces that encompass previous models as special cases and continuously cover the entire range from ductile to brittle. Compact analytic expressions for force-dependent rates and rupture-force distributions allow us to analyze force-clamp and force-ramp pulling experiments. We find that the force-transmitting protein domains of filamin and titin are kinetically ductile when pulled from their two termini, making them resistant to force spikes. For the mechanostable muscle protein titin, a highly ductile model reconciles data over 10 orders of magnitude in force loading rate from experiment and simulation.
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Registered trials
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