ArticleScientific reports2016
Maximum limit to the number of myosin II motors participating in processive sliding of actin.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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9 citing papers in PubMed, 23 citations in OpenAlex.
- Anion and cation fluxes in Escherichia coli during glucose fermentation and their biochemical implications.Scientific reports · 2026Article
- Symmetry breaking and mismatch in the torsional mechanism of ATP synthesis by FTheory in biosciences = Theorie in den Biowissenschaften · 2025Article
- Surface Topography Induces and Orients Nematic Swarms of Active Filaments: Considerations for Lab-On-A-Chip Devices.ACS applied nano materials · 2024Article
- Phosphorus Chemistry at the Roots of Bioenergetics: Ligand Permutation as the Molecular Basis of the Mechanism of ATP Synthesis/Hydrolysis by FMolecules (Basel, Switzerland) · 2023Article
- Elucidating Events within the Black Box of Enzyme Catalysis in Energy Metabolism: Insights into the Molecular Mechanism of ATP Hydrolysis by FBiomolecules · 2023Article
- Solving Exact Cover Instances with Molecular-Motor-Powered Network-Based Biocomputation.ACS nanoscience Au · 2022Article
- Muscle active force-length curve explained by an electrophysical model of interfilament spacing.Biophysical journal · 2022Article
- Myosin II Filament Dynamics in Actin Networks Revealed with Interferometric Scattering Microscopy.Biophysical journal · 2020Article
- Determination of the Maximum Velocity of Filaments in theFrontiers in physiology · 2019Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In this work, we analysed processive sliding and breakage of actin filaments at various heavy meromyosin (HMM) densities and ATP concentrations in IVMA. We observed that with addition of ATP solution, the actin filaments fragmented stochastically; we then determined mean length and velocity of surviving actin filaments post breakage. Average filament length decreased with increase in HMM density at constant ATP, and increased with increase in ATP concentration at constant HMM density. Using density of HMM molecules and length of actin, we estimated the number of HMM molecules per actin filament (N) that participate in processive sliding of actin. N is solely a function of ATP concentration: 88 ± 24 and 54 ± 22 HMM molecules (mean ± S.D.) at 2 mM and 0.1 mM ATP respectively. Processive sliding of actin filament was observed only when N lay within a minimum lower limit (Nmin) and a maximum upper limit (Nmax) to the number of HMM molecules. When N < Nmin the actin filament diffused away from the surface and processivity was lost and when N > Nmax the filament underwent breakage eventually and could not sustain processive sliding. We postulate this maximum upper limit arises due to increased number of strongly bound myosin heads.
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