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. 2017 May 12;7:1822. doi: 10.1038/s41598-017-01604-8

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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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Direct measurements of the effect of Ca⁺⁺ on the rate at which a single myosin molecule binds to a regulated thin filament (RTF). (a) Cartoon of the single molecule laser trap (not to scale). (b) Raw data, showing the position of one of the laser-trapped beads as a function of time. Binding events, indicated with a vertical arrow, are much less frequent at low Ca⁺⁺ (pCa 7) than at high Ca⁺⁺ (pCa 4). (c) Event frequency, scaled by the event frequency in the absence of regulation (2.2 s⁻¹) as a function of Ca⁺⁺ is well-fit by equations (1) and (2), with K = 0.216 μM. Symbols indicate mean frequency, error bars show standard deviation. The data point at pCa 9 is from ref. 28. ATP concentration is 1 μM.