ArticleThe Journal of physiology2012
An integrated in vitro and in situ study of kinetics of myosin II from frog skeletal muscle.
Article in The Journal of physiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 28 citations in OpenAlex.
- Mechanics of blunting of actin-myosin interaction dynamics by the actinopathy-causing mutation E334Q in cytoskeletal γ-actin.The Journal of physiology · 2026Article
- Molecular Events of the Crossbridge Cycle Reflected in the Force-Velocity Relationship of Activated Muscle.Frontiers in physiology · 2022Review
- A Myosin II-Based Nanomachine Devised for the Study of CaInternational journal of molecular sciences · 2020Article
- Determination of the Maximum Velocity of Filaments in theFrontiers in physiology · 2019Article
- Extraction Protocols for Individual Zebrafish's Ventricle Myosin and Skeletal Muscle Actin forFrontiers in physiology · 2017Article
- Is muscle powered by springs or motors?Journal of muscle research and cell motility · 2016Review
- Maximum limit to the number of myosin II motors participating in processive sliding of actin.Scientific reports · 2016Article
- Velocities of unloaded muscle filaments are not limited by drag forces imposed by myosin cross-bridges.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Poorly understood aspects of striated muscle contraction.BioMed research international · 2015Review
- Combining single-molecule manipulation and imaging for the study of protein-DNA interactions.Journal of visualized experiments : JoVE · 2014Article
- Hill's equation of muscle performance and its hidden insight on molecular mechanisms.The Journal of general physiology · 2013Review
- Nonlinear cross-bridge elasticity and post-power-stroke events in fast skeletal muscle actomyosin.Biophysical journal · 2013Article
- Mechanical coupling between myosin molecules causes differences between ensemble and single-molecule measurements.Biophysical journal · 2012Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A new efficient protocol for extraction and conservation of myosin II from frog skeletal muscle made it possible to preserve the myosin functionality for a week and apply single molecule techniques to the molecular motor that has been best characterized for its mechanical, structural and energetic parameters in situ.With the in vitro motility assay, we estimated the sliding velocity of actin on frog myosin II (VF) and its modulation by pH, myosin density, temperature (range 4-30◦C) and substrate concentration. VF was 8.88 ± 0.26 μms⁻¹ at 30.6◦C and decreased to 1.60 ± 0.09 μms⁻¹ at 4.5◦C. The in vitro mechanical and kinetic parameters were integrated with the in situ parameters of frog muscle myosin working in arrays in each half-sarcomere. By comparing VF with the shortening velocities determined in intact frog muscle fibres under different loads and their dependence on temperature, we found that VF is 40-50% less than the fibre unloaded shortening velocity (V0) at the same temperature and we determined the load that explains the reduced value of VF. With this integrated approach we could define fundamental kinetic steps of the acto-myosin ATPase cycle in situ and their relation with mechanical steps. In particular we found that at 5◦C the rate of ADP release calculated using the step size estimated from in situ experiments accounts for the rate of detachment of motors during steady shortening under low loads.
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