Sub-piconewton force fluctuations of actomyosin in vitro
- 1 July 1991
- journal article
- Published by Springer Nature in Nature
- Vol. 352 (6333) , 301-306
- https://doi.org/10.1038/352301a0
Abstract
A new system has been developed for measuring the forces produced by a small number (less than 5-150) of myosin molecules interacting with a single actin filament in vitro. The technique can resolve forces of less than a piconewton and has a time resolution in the submillisecond range. It can thus detect fluctuations of force caused by individual molecular interactions. From analysis of these force fluctuations, the coupling between the enzymatic ATPase activity of actomyosin and the resulting mechanical impulses can be elucidated.Keywords
This publication has 44 references indexed in Scilit:
- Mechanochemical coupling in actomyosin energy transduction studied by in vitro movement assayJournal of Molecular Biology, 1990
- Direction and Speed of Actin Filaments Moving along Thick Filaments Isolated from Molluscan Smooth MuscleThe Journal of Biochemistry, 1990
- Polarity and Velocity of Sliding Filaments: Control of Direction by Actin and of Speed by MyosinScience, 1990
- Bidirectional movement of actin filaments along tracks of myosin headsNature, 1989
- Myosin subfragment-1 is sufficient to move actin filaments in vitroNature, 1987
- Sliding movement of single actin filaments on one-headed myosin filamentsNature, 1987
- Fluorescent actin filaments move on myosin fixed to a glass surface.Proceedings of the National Academy of Sciences, 1986
- Direct observation of motion of single F-actin filaments in the presence of myosinNature, 1984
- Changes in the Cross-Striations of Muscle during Contraction and Stretch and their Structural InterpretationNature, 1954
- Structural Changes in Muscle During Contraction: Interference Microscopy of Living Muscle FibresNature, 1954