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. 2013 Jul 26;8(7):e70636. doi: 10.1371/journal.pone.0070636

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© 2013 Müller et al

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.

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The light scattering signal normalized to the initial value shows the time-dependent dissociation and association of the actomyosin complex formed by NM-2B and α- or γ-actin. The initial drop in the light scattering signal follows the release of ATP from caged-ATP by a flash of UV-laser. The single exponential reduction in scattering intensity monitors the ATP-induced dissociation of myosin from F-actin. The following restoration of the light scattering signal is caused by rebinding of myosin to the actin filament after ATP hydrolysis is completed. As shown for NM-2B, γ-actin causes faster dissociation and association compared to α-actin. Note the logarithmic time scale on the graph.