From Single Molecule Fluctuations to Muscle Contraction: A Brownian Model of A.F. Huxley's Hypotheses
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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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In muscle contraction, release of chemical energy is often accompanied by thermal fluctuation, which can transform muscular force via cyclical myosin-actin interactions.
“In the classic example of muscle contraction as biomolecular machines, the release of chemical energy is often accompanied by thermal fluctuation, which can transform muscular force generated in response to external stimuli through cyclical interactions between myosin and actin.539”
From Protein Ensembles: How Does Nature Harness Thermodynamic Fluctuations for Life? The Diverse Functional Roles of Conformational Ensembles in the Cell (2016) · cites this paper as [539]
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Retracted: A review on biodesalination using halophytic microalgae: opportunities and challenges
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Retracted
- Authors
- Marcucci, L., & Yanagida, T.
- Affiliations
- The University of Osaka (JP)
- RIKEN (JP)
- Corresponding author
- Marcucci, Lorenzo
- ORCID
- Marcucci, Lorenzo
- Venue
- PLoS ONE
- Publisher
- Public Library of Science (PLoS)
- Published
- 2012-07-16
- Volume
- 7
- Issue
- 7
- Pages
- e40042
- ISSN
- 1932-6203 (ISSN-L)
- PMC
- PMC3397984
- OpenAlex
- W2100332633
- Cited by
- 115
- References
- 44
- Citations by year
- 2025: 1 · 2024: 1 · 2023: 2 · 2021: 21 · 2020: 10 · 2019: 13 · 2018: 10 · 2017: 22 · 2016: 16 · 2015: 8 · 2014: 5 · 2013: 4 · 2012: 2
- FWCI
- 3.91
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- PLoS ONE (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Padua Research Archive (University of Padova) (submittedVersion, cc-by)
- RePEc: Research Papers in Economics (submittedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Figshare (submittedVersion, cc-by)
- Funders
- Ministry of Education, Culture, Sports, Science and Technology
- Topics
- Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Cardiomyopathy and Myosin Studies
- Physical Sciences › Physics and Astronomy › Statistical and Nonlinear Physics › Advanced Thermodynamics and Statistical Mechanics
- Physical Sciences › Physics and Astronomy › Statistical and Nonlinear Physics › stochastic dynamics and bifurcation
- Keywords
- muscle contraction, actomyosin, cross-bridge cycling, Huxley model, potential bias, diffusion theory, actin-myosin interaction, muscle force production
- MeSH terms
- Actomyosin, Diffusion, Models, Biological, Muscle Contraction, Sarcomeres, Temperature, Thermodynamics
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Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
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