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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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Stopped-flow kinetic measurements of binding of ^FIFRT IRE-RNA and ^FIACO2 IRE-RNA with IRP1 protein. Representative kinetic data show the time-dependent increase in anisotropy after (A) FRT IRE-RNA and (B) ACO2 IRE-RNA had been mixed with IRP1 at temperature 25 °C and 10 °C. 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 drawn through the data points was fit by assuming a single-exponential process. Residuals for the exponential fits are shown in the bottom panels. The experimental conditions are described in Experimental Procedures.