ArticleProceedings of the National Academy of Sciences of the United States of America2012
Interpreting the widespread nonlinear force spectra of intermolecular bonds.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 88 papers.
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Who cites it
88 citing papers in PubMed.
- Single-Molecule Force Spectroscopy: Experiments, Analysis, and Simulations.Methods in molecular biology (Clifton, N.J.) · 2027Article
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- Ion-Specific Effects of Alkaline Earth Metal Ion Binding to an Anionic Carboxylate Monolayer.Langmuir : the ACS journal of surfaces and colloids · 2026Article
- Chemifriction and Superlubricity: Friends or Foes?The journal of physical chemistry letters · 2025Article
- From viral assembly to host interaction: AFM's contributions to virology.Journal of virology · 2025Review
- Mechanical control of antigen detection and discrimination by T and B cell receptors.Biophysical journal · 2024Review
- Characterization of the interaction between the Sec61 translocon complex and ppαF using optical tweezers.Protein science : a publication of the Protein Society · 2024Article
- Azobenzene as a photoswitchable mechanophore.Nature chemistry · 2024Article
- Molecular-Scale Investigations Reveal the Effect of Natural Polyphenols on BAX/Bcl-2 Interactions.International journal of molecular sciences · 2024Article
- Mechanosensory entities and functionality of endothelial cells.Frontiers in cell and developmental biology · 2024Review
- Relevance of Host Cell Surface Glycan Structure for Cell Specificity of Influenza A Viruses.Viruses · 2023Article
- Combining DNA scaffolds and acoustic force spectroscopy to characterize individual protein bonds.Biophysical journal · 2023Article
- Free energy and kinetic rate calculation via non-equilibrium molecular simulation: application to biomolecules.Biophysical reviews · 2022Review
- Phosphorylation disrupts long-distance electron transport in cytochrome c.Nature communications · 2022Article
- 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
- Measuring biological materials mechanics with atomic force microscopy - Mechanical unfolding of biopolymers.Microscopy research and technique · 2022Article
- Optimal Sacrificial Domains in Mechanical Polyproteins:JACS Au · 2022Article
- Elasticity-associated rebinding rate of molecular bonds between soft elastic media.Biophysical journal · 2022Article
28 more citing papers are in PubMed but not listed here.
Corrections and comments
- Erratum issued
Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Single molecule force spectroscopy probes the strength, lifetime, and energetic details of intermolecular interactions in a simple experiment. A growing number of these studies have reported distinctly nonlinear trends in rupture force with loading rate that are typically explained in conventional models by invoking complex escape pathways. Recent analyses suggested that these trends should be expected even for simple barriers based on the basic assumptions of bond rupture dynamics and thus may represent the norm rather than the exception. Here we explore how these nonlinear trends reflect the two fundamental regimes of bond rupture: (i) a near-equilibrium regime, produced either by bond reforming in the case of a single bond or by asynchronized rupture of multiple individual bonds, and (ii) a kinetic regime produced by fast, non-equilibrium bond rupture. We analyze both single- and multi-bonded cases, describe the full evolution of the system as it transitions between near- and far-from-equilibrium loading regimes, and show that both interpretations produce essentially identical force spectra. Data from 10 different molecular systems show that this model provides a comprehensive description of force spectra for a diverse suite of bonds over experimentally relevant loading rates, removes the inconsistencies of previous interpretations of transition state distances, and gives ready access to both kinetic and thermodynamic information about the interaction. These results imply that single-molecule binding free energies for a vast number of bonds have already been measured.
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