Molecular and subcellular-scale modeling of nucleotide diffusion in the cardiac myofilament lattice.

ABSTRACT: Contractile function of cardiac cells is driven by the sliding displacement of myofilaments powered by the cycling myosin crossbridges. Critical to this process is the availability of ATP, which myosin hydrolyzes during the cross-bridge cycle. The diffusion of adenine nucleotides through the myofilament lattice has been shown to be anisotropic, with slower radial diffusion perpendicular to the filament axis relative to parallel, and is attributed to the periodic hexagonal arrangement of the thin (actin) and thick (myosin) filaments. We investigated whether atomistic-resolution details of myofilament proteins can refine coarse-grain estimates of diffusional anisotropy for adenine nucleotides in the cardiac myofibril, using homogenization theory and atomistic thin filament models from the Pr

SUBMITTER: Kekenes-Huskey PM 

PROVIDER: S-EPMC3835335 | biostudies-literature | 2013 Nov

REPOSITORIES: biostudies-literature