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. 2017 Dec 7;7:17159. doi: 10.1038/s41598-017-17144-0

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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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Structure of the extracellular sequence of C55. (A) Solid-state DARR NMR of intra-residue contacts between Val12 - Leu17 and Tyr10 - Phe19. The C55 peptide labeled with ¹³Cζ-Tyr10, ¹³C1-Val12, ¹³Cα-Leu17 and ¹³C-ring-Phe19 was reconstituted into DMPC:DMPG bilayers as previously described¹⁸. (B) Model of the C55 extracellular region based on FTIR and NMR data showing the regions of the β-secondary structure, Val12 - Leu17 and Tyr10 - Phe19 contacts, and orientations of Phe19-Phe20 relative to the membrane bilayer surface.