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. 2017 Jul 21;8:92. doi: 10.1038/s41467-017-00079-5

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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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Fig. 2 — Side-chain triazole groups disrupt the backbone α-helical conformation. a Chemical structures of PE and PA. b H-bonding pattern analysis of amide, ester, 1,2,3-triazole, and 1,2,3-triazolium. H-bond donors and acceptors are highlighted in red and blue, respectively. c Chemical structures of P1-P3. The molecular design of triazole polypeptides is highlighted, where each component is essential for the study. d, e CD spectra of polypeptides. PE and PA were analyzed at pH 3.0 (d), and P1-P3 were analyzed at pH 7.0 (e)