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. 2017 Nov 27;7:16338. doi: 10.1038/s41598-017-15997-z

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© The Author(s) 2017

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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Sites of cysteine modification are not in regions predicted to be disordered. (a) Predicted folding propensity (in 21 amino acid windows) is shown for benchmark standard sets (STD) of ordered and disordered proteins. Unmodified cysteine sites in sets of proteins that are modified either coincide with the ordered benchmark set or (S-palmitoylated proteins) include regions with greater folding propensity. (b) Cysteine PTM sites approximately coincide with their cognate unmodified sites, with no clear trend towards predicted disorder.