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. 2018 Jul 17;8:10783. doi: 10.1038/s41598-018-28956-z

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© The Author(s) 2018

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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Typical CID profiles (a) showing the decrease in intensity of the [M + 4 H]⁴⁺ peptide: DNA complexes as a function of collision energy (eV), charge (z) and degrees of freedom (DoF). The dissociation threshold (inset) shows the absolute derivative of each CID profiles as a function of the collision energy. The binding affinity (b) and distance matrix (c) illustrates the influence of the single amino acid substitution on the peptide-DNA binding affinity.