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. 2017 Aug 4;18:577. doi: 10.1186/s12864-017-3977-y

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© The Author(s). 2017

Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided 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 Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

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Fig. 5 — The distribution of the lysines in the protein secondary structures and their surface accessibility. (a) The protein secondary structures. (b) The surface accessibility. Succinylated lysines and all lysines were compared in the context of their protein secondary structures (α helix, β strand, and coil) and their relative surface accessibility (RSA). Significance was calculated by Wilcoxon rank-sum test. P< 0.05 was considered significant