ArticleProceedings of the National Academy of Sciences of the United States of America2013
Electrostatic origin of the unidirectionality of walking myosin V motors.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 33 citations in OpenAlex.
- The hypertrophic cardiomyopathy myosin variant G256E prolongs cardiac muscle relaxation via altered nucleotide handling.Communications chemistry · 2026Article
- A tunable autonomous RNA-fueled micro-engine.Nature communications · 2026Article
- Understanding hypertrophic cardiomyopathy and its regulation by myosin drugs.Protein science : a publication of the Protein Society · 2025Article
- How Omecamtiv Modulates Myosin Motion.Biochemistry · 2025Article
- Power Strokes in Molecular Motors: Predictive, Irrelevant, or Somewhere in Between?Journal of the American Chemical Society · 2025Article
- Multicellularity and Electrical Forces.Reviews of physiology, biochemistry and pharmacology · 2025Review
- On the Control of Directionality of Myosin.Journal of the American Chemical Society · 2024Article
- The mechanism of DNA unwinding by the eukaryotic replicative helicase.Nature communications · 2019Article
- The FPhotosynthesis research · 2017Review
- Reexamining the origin of the directionality of myosin V.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Simulating the dynamics of the mechanochemical cycle of myosin-V.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Strain Mediated Adaptation Is Key for Myosin Mechanochemistry: Discovering General Rules for Motor Activity.PLoS computational biology · 2016Article
- The Physics and Physical Chemistry of Molecular Machines.Chemphyschem : a European journal of chemical physics and physical chemistry · 2016Review
- Principles and Overview of Sampling Methods for Modeling Macromolecular Structure and Dynamics.PLoS computational biology · 2016Review
- Irrelevance of the power stroke for the directionality, stopping force, and optimal efficiency of chemically driven molecular machines.Biophysical journal · 2015Article
- Myosin directionality results from coupling between ATP hydrolysis, lever motion, and actin binding.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Response to Vilfan: Constructing structure-based free energy surfaces is the key to understand myosin V unidirectionality.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
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2 authors at 1 institution in 1 country.
Funding
Abstract
Understanding the basis for the action of myosin motors and related molecular machines requires a quantitative energy-based description of the overall functional cycle. Previous theoretical attempts to do so have provided interesting insights on parts of the cycle but could not generate a structure-based free energy landscape for the complete cycle of myosin. In particular, a nonphenomenological structure/energy-based understanding of the unidirectional motion is still missing. Here we use a coarse-grained model of myosin V and generate a structure-based free energy surface of the largest conformational change, namely the transition from the post- to prepowerstroke movement. We also couple the observed energetics of ligand binding/hydrolysis and product release to that of the conformational surface and reproduce the energetics of the complete mechanochemical cycle. It is found that the release in electrostatic free energy upon changing the conformation of the lever arm and the convertor domain from its post- to prepowerstroke state provides the necessary energy to bias the system towards the unidirectional movement of myosin V on the actin filament. The free energy change of 11 kcal is also in the range of ∼2-3 pN, which is consistent with the experimentally observed stalling force required to stop the motor completely on its track. The conformational-chemical coupling generating a successful powerstroke cycle is believed to be conserved among most members of the myosin family, thus highlighting the importance of the previously unknown role of electrostatics free energy in guiding the functional cycle in other actin-based myosin motors.
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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.