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. 2017 Aug 1;7:6976. doi: 10.1038/s41598-017-07072-4

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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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Structural changes in apo and Ca²⁺-bound hSCGN analyzed by hydrogen/deuterium exchange mass spectrometry. (A) Overlay of differential HDX data onto the structures of human SCGN structure which were modeled in silico with the MODELLER 9.9 program. Percentage difference in HDX between apo and Ca²⁺ bound hSCGN is colored according to the key. The differential deuterium exchange patterns of hSCGN peptide sequences representing EF-hand and Cys residue in N-terminal (B) and C-terminal (C) peptides of hSCGN.