ArticleBiophysical journal2013
Effects of ATP and actin-filament binding on the dynamics of the myosin II S1 domain.
Article in Biophysical journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 15 citations in OpenAlex.
- Myosin Post-Translational Modifications Associated With Critical Illness Myopathy.Acta physiologica (Oxford, England) · 2026Article
- The Twisting and Untwisting of Actin and Tropomyosin Filaments Are Involved in the Molecular Mechanisms of Muscle Contraction, and Their Disruption Can Result in Muscle Disorders.International journal of molecular sciences · 2025Review
- The ATP-dependent Pathways and Human Diseases.Current medicinal chemistry · 2023Article
- Mechanochemical Function of Myosin II: Investigation into the Recovery Stroke and ATP Hydrolysis.The journal of physical chemistry. B · 2020Article
- Oxidative hotspots on actin promote skeletal muscle weakness in rheumatoid arthritis.JCI insight · 2019Article
- Multiscale simulation of actin filaments and actin-associated proteins.Biophysical reviews · 2018Review
- Allosteric modulation of cardiac myosin dynamics by omecamtiv mecarbil.PLoS computational biology · 2017Article
- Characterization of the flexibility of the peripheral stalk of prokaryotic rotary A-ATPases by atomistic simulations.Proteins · 2016Article
- Statistical Thermodynamics for Actin-Myosin Binding: The Crucial Importance of Hydration Effects.Biophysical journal · 2016Article
- Cations Stiffen Actin Filaments by Adhering a Key Structural Element to Adjacent Subunits.The journal of physical chemistry. B · 2016Article
- Structural model of weak binding actomyosin in the prepowerstroke state.The Journal of biological chemistry · 2015Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Actin and myosin interact with one another to perform a variety of cellular functions. Central to understanding the processive motion of myosin on actin is the characterization of the individual states along the mechanochemical cycle. We present an all-atom molecular dynamics simulation of the myosin II S1 domain in the rigor state interacting with an actin filament. We also study actin-free myosin in both rigor and post-rigor conformations. Using all-atom level and coarse-grained analysis methods, we investigate the effects of myosin binding on actin, and of actin binding on myosin. In particular, we determine the domains of actin and myosin that interact strongly with one another at the actomyosin interface using a highly coarse-grained level of resolution, and we identify a number of salt bridges and hydrogen bonds at the interface of myosin and actin. Applying coarse-grained analysis, we identify differences in myosin states dependent on actin-binding, or ATP binding. Our simulations also indicate that the actin propeller twist-angle and nucleotide cleft-angles are influenced by myosin at the actomyosin interface. The torsional rigidity of the myosin-bound filament is also calculated, and is found to be increased compared to previous simulations of the free filament.
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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.