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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 helices H3 (S57C) and H5 (V78C). (a) Structural positions of the attached fluorophores onto the specific mutants S57C (H3) and V78C (H5). (b) Unfolding experiments as a function of the GdmCl concentration ascertained by measuring the changes in fluorescence anisotropy for S57C and V78C. Experiments were carried out using 0.1 μM of labelled protein, incubated with different denaturant concentrations at pH 5.0 (black) and 7.8 (red). Data obtained in all experiments were fitted to a three-state monomer unfolding.