Motor-Driven Dynamics in Actin-Myosin Networks
- 14 December 2001
- journal article
- research article
- Published by American Physical Society (APS) in Physical Review Letters
- Vol. 88 (1), 018101
- https://doi.org/10.1103/PhysRevLett.88.018101
Abstract
The effect of myosin motor protein activity on the filamentous actin (F-actin) rheological response is studied using diffusing wave spectroscopy. Under conditions of saturating motor activity, we find an enhancement of longitudinal filament fluctuations corresponding to a scaling of the viscoelastic shear modulus . As the adenosine tri-phosphate reservoir sustaining motor activity is depleted, we find an abrupt transient to a passive, “rigor state” and a return to dissipation dominated by transverse filament modes. Single-filament measurements of the apparent persistence length support the notion that motor activity leads to an increase in the effective temperature for tangential motion.
Keywords
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