Velocity-dependent actomyosin ATPase cycle revealed by in vitro motility assay with kinetic analysis.

ABSTRACT: The actomyosin interaction plays a key role in a number of cellular functions. Single-molecule measurement techniques have been developed to study the mechanism of the actomyosin contractile system. However, the behavior of isolated single molecules does not always reflect that of molecules in a complex system such as a muscle fiber. Here, we developed a simple method for studying the kinetic parameters of the actomyosin interaction using small numbers of molecules. This approach does not require the specialized equipment needed for single-molecule measurements, and permits us to observe behavior that is more similar to that of a complex system. Using an in vitro motility assay, we examined the duration of continuous sliding of actin filaments on a sparsely distributed heavy meromyosin-coa

SUBMITTER: Sato MK 

PROVIDER: S-EPMC3443775 | biostudies-literature | 2012 Aug

REPOSITORIES: biostudies-literature