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. 2017 May 25;7:2429. doi: 10.1038/s41598-017-02677-1

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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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Monitoring of the urea-induced unfolding and refolding of the human PAD4 calcium-binding-site mutant enzymes by CD spectrometry and the intrinsic protein fluorescence. The PAD4 calcium-binding-site mutant enzymes in the presence of 10 mM Ca²⁺ were treated with various concentrations of urea in 50 mM Tris-HCl buffer (pH 7.4) at 25 °C for 16 h and then monitored through CD spectrometry (Panels (A–E)) or fluorescence (Panels (F–J)). Panels (A and F) PAD4_Ca1. Panels (B and G) PAD4_Ca2. Panels (C and H) PAD4_Ca3. Panels (D and I) PAD4_Ca4. Panels (E and J) PAD4_Ca5. Open circles: the PAD4 enzyme was denatured with different concentrations of urea. Closed circles: the PAD4 enzyme was completely denatured with 8 M urea and then renatured by diluting the urea concentration as indicated in the figures. All the data were fitted by either a two-state or three-state model. The fit results and residues are shown as a solid line with error bars.