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. 2016 Feb 3;14:3. doi: 10.1186/s12953-016-0092-y

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© Cheng et al. 2016

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 — Properties of the succinylated peptides. a Succinylation motifs and conservation of succinylation sites. b Heat map of the amino acid compositions of the succinylated site. c Distribution of succinylated lysines and all lysines in protein secondary structures. All the identified 815 succinylation sites (Additional file 1) were used for the analysis. Software motif-x was used to analysis the model of sequences constituted with amino acids in specific positions of succinyl-21-mers (10 amino acids upstream and downstream of the site). The local secondary structures of succinylated proteins were predicted by NetSurfP. P-value < 0.05 was considered significant for these analysis