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. 2017 Aug 17;7:8532. doi: 10.1038/s41598-017-09093-5

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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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Temperature dependent kinetics of IRP1 binding with ^FIFRT IRE-RNA-Mn²⁺ and ^FIACO2 IRE-RNA-Mn²⁺. Representative kinetic data show the time-dependent increase in anisotropy after (A) FRT IRE-RNA-Mn²⁺ and (B) ACO2 IRE-RNA-Mn²⁺ had been mixed with IRP1 protein at temperature 25 °C and 10 °C. Concentration of Mn²⁺ was 50 µM. FRT and ACO2 IRE-RNA concentrations was 50 nM (final) and the IRP1 concentration was 1 µM (final). The solid line represents the fitted curve for single-exponential function. Residuals for the fits are shown in the bottom panels. The experimental conditions are described in Experimental Procedures.