Table 2.

Transition rates for the motor network displayed in Fig. 2 for $F=0$, i.e., in the absence of external load

Rate	${\kappa }_{ij},{\widehat{\kappa }}_{ij}$	Value	Ref.
ATP binding∗	${\widehat{\kappa }}_{23},{\widehat{\kappa }}_{56}$	0.9 (μM s)−1	(24)
ATP release†	${\kappa }_{32},{\kappa }_{65}$	2 × 10−5 s−1	(29)
ADP binding∗	${\widehat{\kappa }}_{21},{\widehat{\kappa }}_{52}$	4.5 (μM s)−1	(7)
ADP release∗	κ12	12 s−1	(24)
ADP release‡	κ25	1.2 s−1	—
P binding†	${\widehat{\kappa }}_{14}$	0.65 (μM s)−1	—
	${\widehat{\kappa }}_{26}$	6 × 10−7 (μM s)−1	—
P release∗	κ41, κ62	250 s−1	(24)
Step	κ34′§	7000 ${\text{s}}^{-1}$	(18)
	κ4′3‡	0.65 s−1	—
	κ55′‡, κ5′5‡	1.5 × 10−8 s−1	—

The experimental values in De La Cruz et al. (24) and Rief et al. (7) have been obtained for monomeric and dimeric myosin V, respectively. A significant discrepancy is found between these two myosins for the binding rate of ADP, which was estimated to be 10–12 (μM s)⁻¹ for monomeric myosin V. In Craig and Linke (18), the value for the stepping rate is referred to as the tethered diffusion rate.

^∗Values obtained from experimental data.

^†Values obtained from balance conditions.

^‡Values obtained by comparison of our calculations with the experimental data.

^§Values obtained from simulations.