Actin filaments on myosin beds: The velocity distribution
- 1 December 1995
- journal article
- research article
- Published by American Physical Society (APS) in Physical Review E
- Vol. 52 (6) , 6573-6579
- https://doi.org/10.1103/physreve.52.6573
Abstract
In vitro studies of actin filaments sliding on a myosin-coated surface are analyzed, filament by filament, at a sampling rate of 30 per second. For each filament, the mean arc length coordinate is computed and histograms of instantaneous velocities, along the arc length, are established. Two types of motion are observed, depending on the experimental conditions. The first one is characterized by a homogeneous flow, with well defined velocities. In this regime, specific defects are a constitutive part of the flow. It is observed at high temperature, at high myosin coverage, and with a particular mode of attachment of myosin to the surface. The second regime shows no clear velocity selection, but a broadband distribution. It is characterized by high friction and is observed at low temperature or low myosin density. (c) 1995 The American Physical SocietyKeywords
This publication has 13 references indexed in Scilit:
- Spiral Defects in Motility Assays: A Measure of Motor Protein ForcePhysical Review Letters, 1995
- Flexibility of myosin attachment to surfaces influences F-actin motionBiophysical Journal, 1995
- How molecular motors workNature, 1994
- Moving forward noisilyNature, 1994
- Factors affecting movement of F-actin filaments propelled by skeletal muscle heavy meromyosinAmerican Journal of Physiology-Cell Physiology, 1992
- Mechanochemical coupling in actomyosin energy transduction studied by in vitro movement assayJournal of Molecular Biology, 1990
- The myosin step size: measurement of the unit displacement per ATP hydrolyzed in an in vitro assay.Proceedings of the National Academy of Sciences, 1990
- Myosin Structure and Function in Cell MotilityAnnual Review of Cell Biology, 1987
- Fluorescent actin filaments move on myosin fixed to a glass surface.Proceedings of the National Academy of Sciences, 1986
- ATP-dependent movement of myosin in vitro: characterization of a quantitative assay.The Journal of cell biology, 1984