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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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Determination of ATP binding and hydrolysis rates for WT and mutant myosin constructs. The binding and subsequent hydrolysis of ATP by Dd myosin-2 induces conformational changes according to Fig. 3, which can be detected by a change of myosin’s intrinsic tryptophan fluorescence. The rate of ATP hydrolysis (k ₊₃ + k ₋₃) was decreased with high significance (p < 0.005) for K265E (see Table 2).