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. 2019 Apr 1;9:5441. doi: 10.1038/s41598-019-41819-5

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© The Author(s) 2019

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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Equilibrium unfolding experiments of wt FoxP1 and H59A mutant. Protein unfolding as a function of denaturant (GdmCl) was monitored using intrinsic fluorescence for wt (a) and H59A (b) at a total protein concentration of 15 μM. (a) wt FoxP1 was incubated with different denaturant concentrations at pH 5.0 (black), 5.5 (blue), 6.0 (brown), 7.0 (green) and 7.8 (red), and the data obtained were fitted to a two-state I $⇆$ U monomer unfolding. (b) The same unfolding experiment was performed with the H59A mutant at pH 5.0, 6.0 and 7.8, using the same colour pattern as for wt protein. Data was fitted to a three-state N₂ $⇆$ 2I $⇆$ 2U unfolding mechanism. Inset. Unfolding curves of the H59A mutant at pH 5.0 using 3 (white circles) or 15 μM (black circles) of total protein concentration. (c) ∆G_u dependence with pH for wt and the H59A mutant. Free energy values for intermediate unfolding (I $⇆$ U) obtained were fitted to Wyman-Tanford relationship (Eq. 2) to calculate the pKa changes between the intermediate and unfolded states.