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. 2017 Nov 30;7:16606. doi: 10.1038/s41598-017-16809-0

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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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Comparison of the synthetic and recombinant human SLURP-1 structural models. (A) Deletion of the methionine (Met0) residue did not significantly alter the overall molecule motility of sSLURP-1 (top). For comparison, rSLURP-1 (bottom) is also presented. Seven superimposed frames from molecular dynamics simulations are shown. The N-terminal region of interest is boxed and the three protruding fingers are labeled I–III. (B) Electrostatic-surface profile of rSLURP-1 (bottom) and sSLURP-1 (top) showing that the positively charged Arg20 is now more solvent exposed. Arrows show regions occupied by Met0 residue in rSLURP-1 or solvent-accessible area in sSLURP-1. (C) Superimposed rSLURP-1 (light brown) and sSLURP-1 (cyan) structures showing the differences in the “head” region where Met0 is located in rSLURP-1. The N-terminal amino groups are indicated by red arrows. In the sSLURP-1 structure, a salt-bridge between residues Lys2 and Asp75 is present (blue arrow). Some residues have been omitted for clarity.