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. 2018 Mar 1;8:3894. doi: 10.1038/s41598-018-22183-2

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© The Author(s) 2018, corrected publication 2021

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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Analysis of physicochemical properties of aggregated proteins. (A) Comparison of the grand average of hydrophobicity (GRAVY) scores as a measure of hydrophobicity. (B) Comparison of Isoelectric points (pI). (C) Comparison of protein size (kDa). Mann–Whiney U-tests were used to assess the statistical significance of observed differences: *p < 0.05, ***p < 0.005. (D) Comparison with proteins that are co-translational substrates of Ssb2³².