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. 2017 Nov 14;7:15544. doi: 10.1038/s41598-017-15299-4

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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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HDX-MS analysis of HvASR1 and TtASR1. The relative fractional uptake was plotted as a function of peptide position for the full-length ASR1 protein, where each color and dot represents a specific time point. The HDX-MS activity for the native proteins is displayed in panel A, in the presence of 10% TFE in Panel B, in the presence of 2 mM ZnSO₄ in Panel C, and in the presence of both 10% TFE and 2 mM in Panel D. Both ASR1 proteins are intrinsically disordered in their native state. Structure formation occurs throughout the proteins in the presence of zinc and TFE, the most dynamic and accessible region of which being located between residues 81 to 115 for HvASR1 and 104 to 113 for TtASR1.