Geometrical correspondence identified and a new interaction unit suggested in striated muscle.
It has long been believed that the periodic structure of the myosin helix is a consequence only of compressing the actin-myosin interaction sites. Here, we identify a length correspondence between the smallest helical unit on the thick filament and the helical pitch of the actin filaments in two different contractile muscles. This suggests a rotation/swing of the filaments that creates a new interaction unit in addition to the single interaction between an actin filament and a myosin head. Numerical characteristics of the single interaction are estimated from discussion about an in vivo interaction utilizing the new unit. The estimated twisted angle of the actin filaments is consistent with that calculated from its torsion rigidity and the evaluated step sizes per cross-bridge can be performed by a single bend of a myosin head. By comparing our evaluated step sizes with experimental results, we conclude that the most plausible mechanism at the force-recovery stage involves swings or rotations of both filaments in the same direction (clockwise).
Nosaka
Michiko
M
Sasebo National College of Technology, Material and Biological Engineering, 1-1 Okishin-chou, Sasebo, Nagasaki 857-1193, Japan. nosaka@post.cc.sasebo.ac.jp
D008841:Actin Cytoskeleton / Q000378:metabolism*; D000199:Actins / Q000032:analysis; D000818:Animals; D001696:Biomechanical Phenomena; D007537:Isometric Contraction / Q000502:physiology; D008954:Models, Biological; D009119:Muscle Contraction / Q000502:physiology*; D018482:Muscle, Skeletal / Q000033:anatomy & histology / Q000378:metabolism*; D009218:Myosins / Q000032:analysis / Q000378:metabolism*; D025941:Protein Interaction Mapping
D000199:Actins; D009218:Myosins