Stepwise sliding of single actin and Myosin filaments.
Dynamics of sliding were explored in isolated actin and myosin filaments. Sliding occurs in steps. The steps are integer multiples of 2.7 nm, which is equal to the monomeric repeat along the actin filament. When filaments were forced to slide in the reverse direction, the size paradigm was the same. This size paradigm is parallel to that seen in the kinesin-microtubule system, where step size is an integer multiple of the tubulin repeat along the microtubule.
Liu
Xiumei
X
Department of Bioengineering, University of Washington, Seattle, Washington 98195, USA.
Pollack
Gerald H
GH
D008841:Actin Cytoskeleton / Q000737:chemistry* / Q000648:ultrastructure; D000199:Actins / Q000737:chemistry* / Q000648:ultrastructure; D000818:Animals; D001665:Binding Sites; D049872:Bivalvia / Q000737:chemistry; D004548:Elasticity; D020409:Molecular Motor Proteins / Q000737:chemistry* / Q000648:ultrastructure; D009038:Motion; D018482:Muscle, Skeletal / Q000737:chemistry; D009218:Myosins / Q000737:chemistry* / Q000648:ultrastructure; D036103:Nanotechnology / Q000295:instrumentation / Q000379:methods; D011485:Protein Binding; D013314:Stress, Mechanical
D000199:Actins; D020409:Molecular Motor Proteins; D009218:Myosins