Motor-driven dynamics in actin-myosin networks

被引：74

作者：

Le Goff, L ^{[1
]}

Amblard, F ^{[1
]}

Furst, EM ^{[1
]}

机构：

[1] Inst Curie, UMR CNRS, IC 168, F-75248 Paris 05, France

来源：

PHYSICAL REVIEW LETTERS | 2002年 / 88卷 / 01期

关键词：

D O I：

10.1103/PhysRevLett.88.018101

中图分类号：

O4 [物理学];

学科分类号：

0702 ;

摘要：

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.

引用

页码：4 / 181014

页数：4

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