Electron microscopy of the actin-myosin head complex in the presence of ATP.
The structure of the actin-myosin head complex during the ATPase cycle has been studied by electron microscopy of negatively stained acto-heavy-meromyosin. In the absence of ATP, heavy meromyosin molecules generally showed a regular, angled appearance, with both heads attached to the actin filament. In the presence of ATP, attached molecules showed a less ordered structure, often with only one head attached. We conclude that configurations other than the rigor structure occur during the actomyosin cross-bridge cycle.
Frado
L L
LL
Department of Cell Biology, University of Massachusetts Medical School, Worcester 01655.
Craig
R
R
D000199:Actins / Q000187:drug effects / Q000648:ultrastructure*; D000255:Adenosine Triphosphate / Q000494:pharmacology*; D000818:Animals; D046911:Macromolecular Substances; D008854:Microscopy, Electron; D009218:Myosins / Q000187:drug effects / Q000648:ultrastructure*; D016624:Negative Staining
D000199:Actins; D046911:Macromolecular Substances; D000255:Adenosine Triphosphate; D009218:Myosins