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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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SDS–PAGE analysis of limited digestion of HvASR1 and TtASR1 by thermolysin both in the presence and absence of 15% TFE at 25 °C. The extent of thermolysin digestion of the purified proteins at different time intervals (0, 1, 3, 6 and 24 h) in the presence of 15% TFE is shown. The extent of digestion of the two proteins, as observed after 1 and 6 h in the absence of TFE is also shown. The black arrow shows undigested ASR1 proteins (1) and the red arrow a fragment resistant to proteolysis (2). M: molecular mass markers. The amino acid sequence of the proteins is shown and the region corresponding to the resistant fragment is shown in red. The underlined region corresponds to the region, shared by both ASR1 proteins, that becomes more structured in the presence of zinc (see also Fig. 11).