Key result
The interaction between single myosin heads and actin monomers is entropy-driven with a binding constant of 10(5) to 10(6) M-1, but produces very small activation of myosin ATPase.
Population
Single myosin heads (subfragment 1) with actin monomers isolated on a solid support
Design
Preclinical
Authors
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Questions single-head sufficiency for cardiac force; leaves open ensemble and regulatory mechanisms in intact sarcomeres.
The interaction between single myosin heads and actin monomers is entropy-driven with high affinity but results in minimal myosin ATPase activation.
Chantler et al. (1976) studied Actomyosin interaction (in vitro). Actin monomers on a solid support was evaluated on Binding constant and thermodynamic properties. The interaction between single myosin heads and actin monomers is entropy-driven with a binding constant of 10(5) to 10(6) M-1, but produces very small activation of myosin ATPase.
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