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. 2020 May 12;10:7896. doi: 10.1038/s41598-020-64135-9

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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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Residual secondary structure propensities (SSPs) in CsgA transition away from PPII helices upon truncation of N₂₂. (A) Outside of random coil, full-length CsgA displays a predominantly PPII helix structure. Small β-sheet propensities are noted in the repeat regions. (B) CsgA_ΔN22 has a reduced PPII helix density, with a significant α-helix propensity appearing between R1 and R2. SSPs are represented by stacked bar plots, with colours showing the relative propensity at each residue, as in the legend. Random coil propensity, the dominant structure in IDPs, is not actively displayed. Regions highlighted red on the plots align with the repeat regions in the sequence schematic above.