ArticleBiophysical journal2012
Velocity-dependent actomyosin ATPase cycle revealed by in vitro motility assay with kinetic analysis.
Article in Biophysical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Cell Behavioral Dynamics as a Cue in Optimizing Culture Stabilization in the Bioprocessing of Pluripotent Stem Cells.Bioengineering (Basel, Switzerland) · 2022Review
- A small-molecule modulator of cardiac myosin acts on multiple stages of the myosin chemomechanical cycle.The Journal of biological chemistry · 2017Article
- Correlated receptor transport processes buffer single-cell heterogeneity.PLoS computational biology · 2017Article
- Maximum limit to the number of myosin II motors participating in processive sliding of actin.Scientific reports · 2016Article
- Single turnovers of fluorescent ATP bound to bipolar myosin filament during actin filaments sliding.Biophysics (Nagoya-shi, Japan) · 2013Article
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The actomyosin interaction plays a key role in a number of cellular functions. Single-molecule measurement techniques have been developed to study the mechanism of the actomyosin contractile system. However, the behavior of isolated single molecules does not always reflect that of molecules in a complex system such as a muscle fiber. Here, we developed a simple method for studying the kinetic parameters of the actomyosin interaction using small numbers of molecules. This approach does not require the specialized equipment needed for single-molecule measurements, and permits us to observe behavior that is more similar to that of a complex system. Using an in vitro motility assay, we examined the duration of continuous sliding of actin filaments on a sparsely distributed heavy meromyosin-coated surface. To estimate the association rate constant of the actomyosin motile system, we compared the distribution of experimentally obtained duration times with a computationally simulated distribution. We found that the association rate constant depends on the sliding velocity of the actin filaments. This technique may be used to reveal new aspects of the kinetics of various motor proteins in complex systems.
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Registered trials
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