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. 2018 Dec 28;19(Suppl 17):494. doi: 10.1186/s12859-018-2462-1

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© The Author(s) 2018

Open Access This 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. 2 — Outline of the experimental design. Raw MS data are converted to deconvoluted mass spectra, which are further searched against the K12 and ISC11 proteome databases separately. A K12 protein segment is obtained from each K12 proteoform identified from the K12 proteome database and searched against the ISC11 proteome database to find the best homologous ISC11 protein by BLAST-P. Then a global-local alignment between the homologous ISC11 protein sequence and the K12 protein segment is used to find the best-scoring homologous protein segment. Finally, homologous protein segments and ISC11 protein segments identified from the ISC11 proteome database are compared to evaluate the accuracy of the ISC11 protein segments, and ISC11 proteoforms are compared with K12 proteoforms to evaluate the accuracy of mass shift localization