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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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ADP inhibition of ATP-induced dissociation of acto-myosin complexes for WT and K265E. (a) The inhibition of the ATP-induced dissociation of the acto-myosin complex was followed by the exponential decrease in the light scattering signal. The graph shows sample traces for the WT at 50 and 800 µM ADP. (b) The plot of the observed rate constants versus the ADP concentration was fit by a hyperbola to give k _-AD and K _AD. The error bars report the standard deviation for three independent experiments (see Table 2).