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. 2019 Feb 21;9:2530. doi: 10.1038/s41598-018-38401-w

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© The Author(s) 2019

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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Secondary structural transition observed for all the systems within 100 ns. (A) Time dependence of β-structure. Maximum (14–16%) β-structure was observed for Wild-type and S7A peptides and minimum (>6%) was observed for I5A peptide oligomers. (B) Time dependence of helical structure formation. Maximum (16–20%) helical content was observed for G3A and I5A, while for all other analogs the content was less than 12%. The percent of helix and β-sheet was calculated using DSSP.