| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10881886 | Cell Biology International | 2005 | 4 Pages |
Abstract
Myosin II controls the viscoelastic behavior of actin filaments, interacting with actin in an energy-dependent manner. Replacing adenosine triphosphate with adenosine diphosphate changes actomyosin sliding to cross-linking. Rheological measurements show a 3-4-fold increase of the elastic portion Gâ² in actin filaments when myosin II is present at a molar ratio rMA=1:200. This observation is supported by the demonstration of inactive myosin heads along actin filaments using atomic force microscopy.
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Authors
Wolfgang H. Goldmann, Horacio F. Cantiello, Bernard Chasan,