Sarcomere lattice geometry influences cooperative myosin binding in muscle.

ABSTRACT: In muscle, force emerges from myosin binding with actin (forming a cross-bridge). This actomyosin binding depends upon myofilament geometry, kinetics of thin-filament Ca(2+) activation, and kinetics of cross-bridge cycling. Binding occurs within a compliant network of protein filaments where there is mechanical coupling between myosins along the thick-filament backbone and between actin monomers along the thin filament. Such mechanical coupling precludes using ordinary differential equation models when examining the effects of lattice geometry, kinetics, or compliance on force production. This study uses two stochastically driven, spatially explicit models to predict levels of cross-bridge binding, force, thin-filament Ca(2+) activation, and ATP utilization. One model incorporates the 2-to

SUBMITTER: Tanner BC 

PROVIDER: S-EPMC1914368 | biostudies-literature | 2007 Jul

REPOSITORIES: biostudies-literature