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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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Bioinformatics insights to cysteine reactivity. (a) Depletion of cysteine at α-helical amino-termini, relative to aspartic acid and serine, suggests that cysteine reactivity is modulated in evolution. Where Cys at a helical N-terminus does occur, and where this is adjacent to an enzyme active (or other modulatory) site, scope exists for targeting with covalent inhibitors. (b) S-palmitoylation sites in particular are enriched for a positively-charged sequence surround, which could lower the Cys pKa, leading to more favourable transfer from the DHHC domain of a PAT. (c) Most notably for sites of S-nitrosylation and S-glutathionylation, about half of modified sites are buried in native structure, and sites are enriched for proximity to lysine ubiquitinations. One possibility is that cysteine modification could be linked to UPS-mediated degradation.