ArticleThe Journal of chemical physics2012
Multiple barriers in forced rupture of protein complexes.
Article in The Journal of chemical physics, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
12 citing papers in PubMed, 30 citations in OpenAlex.
- 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
- Forced-rupture of cell-adhesion complexes reveals abrupt switch between two brittle states.The Journal of chemical physics · 2018Article
- Denaturants Alter the Flux through Multiple Pathways in the Folding of PDZ Domain.The journal of physical chemistry. B · 2018Article
- Kinetic Ductility and Force-Spike Resistance of Proteins from Single-Molecule Force Spectroscopy.Biophysical journal · 2016Article
- Protein Ensembles: How Does Nature Harness Thermodynamic Fluctuations for Life? The Diverse Functional Roles of Conformational Ensembles in the Cell.Chemical reviews · 2016Review
- Force-dependent switch in protein unfolding pathways and transition-state movements.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- On artifacts in single-molecule force spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Investigation of the heparin-thrombin interaction by dynamic force spectroscopy.Biochimica et biophysica acta · 2015Article
- Evidence of disorder in biological molecules from single molecule pulling experiments.Physical review letters · 2014Article
- Force-induced unzipping transitions in an athermal crowded environment.The journal of physical chemistry. B · 2013Article
- Catch bond-like kinetics of helix cracking: network analysis by molecular dynamics and milestoning.The Journal of chemical physics · 2013Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
Abstract
Curvatures in the most probable rupture force (f*) versus log-loading rate (log r(f)) observed in dynamic force spectroscopy (DFS) on biomolecular complexes are interpreted using a one-dimensional free energy profile with multiple barriers or a single barrier with force-dependent transition state. Here, we provide a criterion to select one scenario over another. If the rupture dynamics occurs by crossing a single barrier in a physical free energy profile describing unbinding, the exponent ν, from (1 - f*/f(c))(1/ν) ~ (log r(f)) with f(c) being a critical force in the absence of force, is restricted to 0.5 ≤ ν ≤ 1. For biotin-ligand complexes and leukocyte-associated antigen-1 bound to intercellular adhesion molecules, which display large curvature in the DFS data, fits to experimental data yield ν < 0.5, suggesting that if ligand unbinding is assumed to proceed along one-dimensional pulling coordinate, the dynamics should occur in a energy landscape with multiple-barriers.
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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.