title: Sub-piconewton force fluctuations of actomyosin in vitro.
abstract: A new system has been developed for measuring the forces produced by a small number (less than 5-150) of myosin molecules interacting with a single actin filament in vitro. The technique can resolve forces of less than a piconewton and has a time resolution in the submillisecond range. It can thus detect fluctuations of force caused by individual molecular interactions. From analysis of these force fluctuations, the coupling between the enzymatic ATPase activity of actomyosin and the resulting mechanical impulses can be elucidated.
authors.affiliation: Department of Biophysical Engineering, Osaka University, Japan.
authors.forename: A
authors.initials: A
authors.lastname: Ishijima
authors.forename: T
authors.initials: T
authors.lastname: Doi
authors.forename: K
authors.initials: K
authors.lastname: Sakurada
authors.forename: T
authors.initials: T
authors.lastname: Yanagida
mesh_terms: D000199:Actins / Q000502:physiology; D000205:Actomyosin / Q000502:physiology*; D000251:Adenosine Triphosphatases / Q000378:metabolism; D006801:Humans; D066298:In Vitro Techniques; D008433:Mathematics; D008722:Methods; D009119:Muscle Contraction; D009218:Myosins / Q000502:physiology
chemical_list: D000199:Actins; D000205:Actomyosin; D000251:Adenosine Triphosphatases; D009218:Myosins