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. 2019 Mar 6;9:3676. doi: 10.1038/s41598-019-39905-9

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© The Author(s) 2019

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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Multidomain UMS pipeline depicting automated processing. (1) Protein domain information is retrieved from UniProt, and (2) domains are homology-modeled, equilibrated in 2 ns of molecular dynamics, compared with an internal control, and subjected to UMS. (3) Sets of homologous domains from each protein are superimposed, and their UMS data are averaged. Foldability and p-values from the averaged UMS data are used to identify critical residues for each domain, and (4) analysis is performed.