Mechanical coupling between myosin molecules causes differences between ensemble and single-molecule measurements.

ABSTRACT: In contracting muscle, individual myosin molecules function as part of a large ensemble, hydrolyzing ATP to power the relative sliding of actin filaments. The technological advances that have enabled direct observation and manipulation of single molecules, including recent experiments that have explored myosin's force-dependent properties, provide detailed insight into the kinetics of myosin's mechanochemical interaction with actin. However, it has been difficult to reconcile these single-molecule observations with the behavior of myosin in an ensemble. Here, using a combination of simulations and theory, we show that the kinetic mechanism derived from single-molecule experiments describes ensemble behavior; but the connection between single molecule and ensemble is complex. In particular,

SUBMITTER: Walcott S 

PROVIDER: S-EPMC3414898 | biostudies-literature | 2012 Aug

REPOSITORIES: biostudies-literature