ArticlePloS one2012
From single molecule fluctuations to muscle contraction: a Brownian model of A.F. Huxley's hypotheses.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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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
10 citing papers in PubMed.
- The Evolution of Large Organism Size: Disparate Physiologies Share a Foundation at the Smallest Physical Scales.Life (Basel, Switzerland) · 2025Review
- Life's Mechanism.Life (Basel, Switzerland) · 2023Review
- Ultra-fast force-clamp spectroscopy data on the interaction between skeletal muscle myosin and actin.Data in brief · 2019Article
- Basic science and clinical use of eccentric contractions: History and uncertainties.Journal of sport and health science · 2018Review
- Single molecule detection, thermal fluctuation and life.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2017Review
- Including Thermal Fluctuations in Actomyosin Stable States Increases the Predicted Force per Motor and Macroscopic Efficiency in Muscle Modelling.PLoS computational biology · 2016Article
- Protein Ensembles: How Does Nature Harness Thermodynamic Fluctuations for Life? The Diverse Functional Roles of Conformational Ensembles in the Cell.Chemical reviews · 2016Review
- Mechanosensing in Myosin Filament Solves a 60 Years Old Conflict in Skeletal Muscle Modeling between High Power Output and Slow Rise in Tension.Frontiers in physiology · 2016Article
- Coupling of lever arm swing and biased Brownian motion in actomyosin.PLoS computational biology · 2014Article
- Muscle contraction mechanism based on single molecule measurements.Journal of muscle research and cell motility · 2012Article
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Muscular force generation in response to external stimuli is the result of thermally fluctuating, cyclical interactions between myosin and actin, which together form the actomyosin complex. Normally, these fluctuations are modelled using transition rate functions that are based on muscle fiber behaviour, in a phenomenological fashion. However, such a basis reduces the predictive power of these models. As an alternative, we propose a model which uses direct single molecule observations of actomyosin fluctuations reported in the literature. We precisely estimate the actomyosin potential bias and use diffusion theory to obtain a brownian ratchet model that reproduces the complete cross-bridge cycle. The model is validated by simulating several macroscopic experimental conditions, while its interpretation is compatible with two different force-generating scenarios.
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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.