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. 2012 Aug 8;103(3):501–510. doi: 10.1016/j.bpj.2012.06.031

Figure 5.

Figure 5

Comparison between theoretical calculations and simulations for actin speed (V), myosin attachment time (T), and attachment distance (D), all normalized to the single-molecule values (single-molecule values are shown as a thin, solid line). These plots are shown as a function of the nondimensional mechanochemical coupling parameter E. Simulations were performed with large ensembles (N = 400) with kinetic parameters based on smooth muscle and skeletal muscle. The value E was varied by using different myosin stiffness values and/or force dependence. (Dashed lines) Our best estimate of E. Theoretical calculations, described in the text and the Supporting Material, agree with the simulations.