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. 2017 Sep 14;7:11596. doi: 10.1038/s41598-017-11984-6

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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 kinetics of mT to Myo19-3IQ and Acto·Myo19-3IQ by monitoring FRET upon tryptophan excitation to mant-fluorophore. (A) Time courses of mT fluorescence change after mixing 200 nM myosin 19-3IQ with 2 (a), 4, (b), 5 (c), 10 µM (d) mT (final concentrations). The smooth lines are the best fit to a single exponential. (B) The dependence of k _obs on [mT]. The solid line through the data points is the best fits to linear equation. Error bars represent standard deviation from three independent experiments. (C) The dependence of the amplitudes on [mT]. The solid lines through the data points are the best fits to linear equation. Error bars of the fitting are within the data points. (D) The dependence of signal to noise ratio (SNR) of the experimental data on [mT]. Note the fast decrease in observable signals. (F) The kinetic reaction mechanism for mT binding to Myo19-3IQ and for Acto·Myo19-3IQ. We included in rectangular parenthesis a rapid collision complex that most likely occurs without fluorescence change.