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Motor-driven dynamics in actin-myosin networks

Author(s)
Le Goff, LAmblard, FFurst, EM
Issued Date
2002-01
DOI
10.1103/PhysRevLett.88.018101
URI
https://scholarworks.unist.ac.kr/handle/201301/31093
Fulltext
https://journals.aps.org/prl/abstract/10.1103/PhysRevLett.88.018101
Citation
PHYSICAL REVIEW LETTERS, v.88, no.1, pp.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 G(d)(omega) similar to omega(7/8). 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.
Publisher
AMERICAN PHYSICAL SOC
ISSN
0031-9007
Keyword
CONCENTRATED ISOTROPIC SOLUTIONSF-ACTINSEMIFLEXIBLE POLYMERSMICROSCOPIC VISCOELASTICITYTHERMAL FLUCTUATIONSMEMBRANESMICRORHEOLOGYMECHANICSTWEEZERSPROTEINS

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