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. 2017 Jul 20;7:6049. doi: 10.1038/s41598-017-06213-z

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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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Sequence analysis, purification and secondary structure elements of recombinant Par h 1. (a) Sequence alignment of defensin-like domains obtained with the multiple sequence alignment program Clustal Omega (b), comparison of proline-rich regions. Art v 1 from Artemisia vulgaris (Q84ZX5), Amb a 4 from Ambrosia artemisiifolia (D4IHC0) and SF18 from Helianthus annuus (P22357) were included. Conserved cysteine residues boxed in grey, conserved residues of defensin-like proteins in bold, proline clusters underlined. The symbols shown in the alignment correspond with identical amino acids (*), conserved substitutions (:), and semi-conserved substitutions (.). (c) Purification process of recombinant Par h 1: BE, bacterial extract; ASP, ammonium sulfate precipitation; HIC1 and HIC2, hydrophobic interaction chromatography and SEC, size exclusion chromatography. (d) Circular dichroism spectra of purified Par h 1. The unprocessed gel is shown in the Related Manuscript File.