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. 2017 Aug 11;7:7954. doi: 10.1038/s41598-017-08402-2

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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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¹³C-¹⁹F distances are measured using ¹⁹F-dephased and ¹³C-detected REDOR spectra of the PFA-tagged π-clamp peptides. Representative spectra were shown. (a) ¹³C CP-MAS spectra of the fully labeled peptide 6, showing the aliphatic (right) and aromatic (left) region. Full intensity (S₀, black) and dephased (S, red) REDOR spectra at a REDOR mixing time of 4 ms for the F1-only labeled π-clamp peptide 7 (b) and P3F4-only labeled peptide 8 (c) are shown. (d) Experimental S/S₀ dephasing values for four representative ¹³C resonances.