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. 2021 Apr 23;153(7):e202012811. doi: 10.1085/jgp.202012811

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© 2021 Rasicci et al.

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Figure 4. — ATP-induced dissociation from actin. The experiment was performed by mixing a complex of M2β-S1 and pyrene actin with increasing concentrations of ATP (5–125 µM). (A and B) The fluorescence transients were best fit by a single exponential function at all ATP concentrations. Representative fluorescence transients at 5 µM ATP (A; k_obs = 36.0 ± 0.2 and 31.1 ± 0.3 s^–1 in WT and K104E, respectively) and 125 µM ATP (B; k_obs = 553.6 ± 18.5 and 403.3 ± 12.0 s^–1 in WT and K104E, respectively). (C) The second-order rate constant K’_1Tk’₊₂ was determined from the linear-dependence on ATP concentration at low ATP concentrations (5–20 µM). (D) The maximal rate of ATP-induced dissociation (k’_+2T) was determined from the hyperbolic fit of k_obs as a function of ATP concentration. AU, arbitrary unit.