A self-induced translation model of myosin head motion along thin filament in muscle contraction.
Evidence has been accumulating that muscle contraction may not be associated with the power stroke of the cross-bridges tightly coupled with ATP hydrolysis cycle. We have constructed a new contraction model which includes a number of basic properties of contraction processes not taken into consideration in the models hitherto reported. The basic assumption is that, when one head of a myosin molecule attaches to an actin monomer on thin filament, conformational changes take place in the neighbouring actin monomers to result in their non-symmetrical charge distribution to exert electrostatic force on the unattached head of the same myosin molecule in one direction. Thus, the unattached head moves along thin filament to attach to another actin monomer, while the already attached head detaches from thin filament. These steps are repeated to cause muscle contraction. The above contraction model can explain the results of our X-ray diffraction experiments as well as the results reported by other authors.
Mitsui
T
T
Department of Biophysical Engineering, Faculty of Engineering Science, Osaka University, Japan.
Wakabayashi
K
K
Tanaka
H
H
Kobayashi
T
T
Amemiya
Y
Y
Iwamoto
H
H
Wang
E Z
EZ
Hamanaka
T
T
Sugi
H
H
D008841:Actin Cytoskeleton / Q000502:physiology; D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D066298:In Vitro Techniques; D008954:Models, Biological; D009119:Muscle Contraction; D009132:Muscles / Q000502:physiology*; D009218:Myosins / Q000378:metabolism*; D011487:Protein Conformation
D000255:Adenosine Triphosphate; D009218:Myosins