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. 2021 Feb 18;50(2):223–237. doi: 10.1007/s00249-020-01490-5

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© The Author(s) 2021

Open AccessThis 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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 7 — Adsorption isotherms of E-peptides recognized by surface bound K-lipopeptides (K-LP) obtained from ellipsometry measurements. Bilayers consisted of DOPC/MCCDOPE 97:3, and K-peptides were covalently coupled to the bilayer surface. a Parallel coiled-coil formation. Solid circles: LP-K3Cys + E3Cys; solid triangles: LP-i-K3Cys + i-E3Cys; data were fitted according to a Langmuir isotherm. b Antiparallel coiled-coil formation. Open circles: LP-K3Cys + i-E3Cys; open triangles: LP-i-K3Cys + E3Cys. A Langmuir isotherm was fit to the data for LP-i-K3Cys + E3Cys, while a Bragg–Williams isotherm was fit to data for LP-K3Cys + i-E3Cys (fits:gray line) (adapted from Pähler et al. (2012))