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• W2011463750 abstract "Unloaded shortening speeds, V, of muscle are thought to be limited by actin-bound myosin heads that resist shortening, or V = a · d · τ on −1 where τ on −1 is the rate at which myosin detaches from actin and d is myosin’s step size. The a-term describes the efficiency of force transmission between myosin heads, and has been shown to become less than one at low myosin densities in a motility assay. Molecules such as inorganic phosphate (P i ), and blebbistatin inhibit both V and actin-myosin strong binding kinetics suggesting a link between V and attachment kinetics. To determine whether these small molecules slow V by increasing resistance to actin sliding or by decreasing the efficiency of force transmission, a, we determine how inhibition of V by P i and blebbistatin changes the force exerted on actin filaments during an in vitro sliding assay, measured from changes in the rate, τ break −1 , at which actin filaments break. Upon addition of 30 mM P i to a low (30 μM) [ATP] motility buffer V decreased from 1.8 to 1.3 μm s−1 and τ break −1 from 0.029 to 0.018 s−1. Upon addition of 50 μM blebbistatin to a low [ATP] motility buffer, V decreased from 1.0 to 0.7 μm s−1 and τ break −1 from 0.059 to 0.022 s−1. These results imply that blebbistatin and P i slow V by decreasing force transmission, a, not by increasing resistive forces, implying that actin-myosin attachment kinetics influence V." @default.
• W2011463750 created "2016-06-24" @default.
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• W2011463750 date "2013-03-01" @default.
• W2011463750 modified "2023-10-17" @default.
• W2011463750 title "Actin Sliding Velocities are Influenced by the Driving Forces of Actin-Myosin Binding" @default.
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• W2011463750 doi "https://doi.org/10.1007/s12195-013-0274-y" @default.
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