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. 2017 Aug 9;7:7650. doi: 10.1038/s41598-017-07933-y

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© The Author(s) 2017

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Binding and release of F-actin. Interaction of F-actin with WT and mutant myosin was followed using pyrene-labelled F-actin. (a) The actin concentration-dependent increase in the observed rate constants for pyrene-actin binding could be fit by a linear function. The slope defines the actin binding rate k _+A, which is slightly decreased by mutations K265E and K265Q. Error bars give the standard deviation for three independent experiments. (b) Fluorescence transients observed after chasing pyrene-actin from the complex with myosin by excess unlabelled F-actin. Single exponential fits to the data define F-actin release rate constants, which are significantly increased for all three mutant myosins. All resulting kinetic parameters for F-actin binding and release are summarized in Table 2.