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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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Dissociation-reassociation of human PAD4 WT and the calcium-binding-site mutant enzymes. The PAD4 WT and the calcium-binding-site mutant enzymes were treated with 1.2 M urea in 50 mM Tris-HCl buffer (pH 7.4) at 25 °C for 16 h, and the protein samples were then diluted 10-fold to reduce the urea concentration to 0.12 M. (A) PAD4_WT. (B) PAD4_Ca1. (C) PAD4_Ca2. (D) PAD4_Ca3. (E) PAD4_Ca4. (F) PAD4_Ca5. Blue line: the enzyme treated with 1.2 M urea. Red line: 10-fold dilution of the 1.2 M urea-treated enzyme (0.12 M urea).