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. 2018 Apr 5;1:23. doi: 10.1038/s42003-018-0027-5

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© The Author(s) 2018

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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Fig. 3 — Unfolding pattern confirms the native fold of OmpG in OMVs. a Density map of 46 superimposed force-distance curves recorded from OMVs collected from E. coli overexpressing OmpG. b Density map of 33 superimposed force-distance curves recorded of OmpG reconstituted in lipid bilayers assembled from E. coli polar lipid extract. Blue (a) and red (b) curves are worm-like chain (WLC) curves indicating the mean contour length of each unfolding force peak. Contour lengths are given in number of amino acids above the WLC curves. c Force vs. contour length plot showing the fitting results of every detected force peak in all force-distance curves. Blue dots are from the measurements on OMVs shown in (a), red dots are from measurements on reconstituted OmpG shown in (b). Each dot represents the analysis of one unfolding force peak. SMFS was recorded in buffer solution (DPBSS) at room temperature (see Methods)