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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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2D ¹³C-¹³C correlation spectra of the (a) unreacted π-clamp peptide 5 and (b) PFA-tagged peptide 6. The spectra were acquired at 298 K. (c,d) Enlarged regions showing Pro3 and Cys2 cross peaks. The Cys2 Cβ chemical shift indicates that Cys2 is in a reduced state (~25 ppm) in peptide 5 (c), and in an oxidized state (~40 ppm) in the PFA-tagged peptide 6 (d). The chemical shift difference between Pro Cβ and Cγ indicates the isomer state. The Pro intensity in (c) indicates an about 1:1 ratio between the cis and trans isomers in the unreacted peptide 5. The Pro signal in (d) shows only the trans Pro conformation is adopted in PFA-tagged peptide 6.