Fig. 7: Single molecule stiffness of acto-MYO6S267E/WT through the cycle. | Nature Communications

Fig. 7: Single molecule stiffness of acto-MYO6S267E/WT through the cycle.

From: Motor ___domain phosphorylation increases nucleotide exchange and turns MYO6 into a faster and stronger motor

Fig. 7

a Schematic of single molecule stiffness measurements. b Schematic and experimental time courses of the ensemble-averaged stiffness of the acto.MYO6 complex measured for MYO6WT and MYO6S267E, see also Fig. 4. c Load-dependent rates k1 and k2 describe the change in stiffness of the acto.MYO6S267E complex at 100 µM ATP at different loads. Light and dark grey circles, k1 and k2 from ≈30 measurements at 100 µM ATP and different loads (mean ± StdErr), see also Fig. 4. Solid lines are fitted using k = ko exp(−Fd/kT), with ko rate at zero load, F force, d distance parameter and kT thermal energy; d1 = 1.8 nm, d2 = 2.8 nm. Extrapolated load-dependent rate \({k}_{2}^{*}\) at 1 mM ATP (dotted line) and \({k}_{2}^{*\ast }\) at 2 mM ATP (dashed line). Source data are provided as a Source Data file.

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