Cooperative conformational change in F-actin filament induced by the binding of heavy meromyosin.
The binding of HMM to F-actin containing bound 1, N6-ethenoadenosine diphosphate (epsilon-ADP), a fluorescent analogue of ADP, caused a significant increase in the fluorescence intensity of epsilon-ADP at 410 nm on excitation at 340 nm. This increase is regarded as due to a conformational change in the actin molecule induced by HMM binding. The fluorescence intensity increase was not directly proportional to the amount of bound HMM. This phenomenon suggests that a conformational change in neighbouring actin molecules is induced cooperatively by the conformational change of the actin molecule binding HMM.
D000199:Actins; D000244:Adenosine Diphosphate / Q000031:analogs & derivatives; D000818:Animals; D001665:Binding Sites; D007700:Kinetics; D046911:Macromolecular Substances; D008433:Mathematics; D009132:Muscles; D015879:Myosin Subfragments; D011485:Protein Binding; D011487:Protein Conformation; D011817:Rabbits; D013050:Spectrometry, Fluorescence
D000199:Actins; D046911:Macromolecular Substances; D015879:Myosin Subfragments; D000244:Adenosine Diphosphate