title: Molecular organizations of myofibrils of skeletal muscle studied by atomic force microscopy.
abstract: By applying AFM technology, we studied mechanical characteristics of myofibrils of skeletal muscle. The obtained results indicate that (1) the Z-band is the most rigid sarcomere component stabilizing the myofibril structures, (2) various filamentous components are inter-connected in sarcomere with sufficient mechanical strength to support the contractile force, and (3) the molecular structure of the overlap region between actin and myosin filaments is anisotropic. In any case the present studies clearly indicate that the AFM technique is a powerful tool to investigate the mechanical characteristics of sarcomere structure of muscle fiber.
authors.affiliation: Department of Physics (Biophysics Section), Faculty of Science, Science University of Tokyo, Shinjuku-ku, Tokyo 162-8601, Japan.
authors.forename: Takenori
authors.initials: T
authors.lastname: Yamada
authors.forename: Yuki
authors.initials: Y
authors.lastname: Kunioka
authors.forename: Jun'ichi
authors.initials: J
authors.lastname: Wakayama
authors.forename: Momoko
authors.initials: M
authors.lastname: Aimi
authors.forename: Yu-suke
authors.initials: YS
authors.lastname: Noguchi
authors.forename: Nao
authors.initials: N
authors.lastname: Akiyama
authors.forename: Taisuke
authors.initials: T
authors.lastname: Kayamori
mesh_terms: D000199:Actins / Q000737:chemistry; D000818:Animals; D016880:Anisotropy; D002478:Cells, Cultured; D018625:Microscopy, Atomic Force / Q000379:methods*; D018482:Muscle, Skeletal / Q000378:metabolism*; D009210:Myofibrils / Q000737:chemistry* / Q000378:metabolism; D009218:Myosins / Q000737:chemistry; D016658:Psoas Muscles / Q000166:cytology; D011817:Rabbits; D012518:Sarcomeres / Q000378:metabolism; D012984:Software
chemical_list: D000199:Actins; D009218:Myosins