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. 2020 Jan 21;10:891. doi: 10.1038/s41598-020-57713-4

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© The Author(s) 2020

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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The effect of scaffolds on peptide immobilisation (a) RMSF profiling of 18 CSA hexapeptides. Average RMSF values of less or more than 1.5 Å are shown by grey- or magenta-coloured squares, respectively. (b) Structural motifs of the flanked loops containing the GA sites. SLS, strand-loop-strand; HLH, helix-loop-helix; SLH, strand-loop-helix; HLS, helix-loop-strand; SLC, strand-loop-cysteine; CLH, cysteine-loop-helix; CLS: cysteine-loop-strand. (c) Distance distribution between Cα atoms of the first and sixth amino acids of hexapeptides in the GA sites.