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 [Formula presented]. 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. © 2002 The American Physical Society.
CITATION STYLE
Le Goff, L., Amblard, F., & Furst, E. M. (2002). Motor-Driven Dynamics in Actin-Myosin Networks. Physical Review Letters, 88(1), 4. https://doi.org/10.1103/PhysRevLett.88.018101
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