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. 2018 Nov 20;8:17111. doi: 10.1038/s41598-018-35383-7

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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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Comparison of the molecular dynamic simulation (MD) of the 150, 123, and 79 amino acid vasoinhibins. (a) Trajectory analysis of PRL and vasoinhibins of 150, 123 and 79 amino acids (Vi150, Vi123, and Vi79, respectively) during 20 ns of MD simulation. Average radius of gyration (Rg), surface area, and root mean square deviation (RMSD) of three MD simulations per molecule. (b) Mean ± SEM root mean square fluctuation (RMSF) per residue of three independent MD simulations. (c) RMSF values in the L1 region. Values of each PRL residue are statistically different (p < 0.05) from both Vi150 and Vi123 (*), or only from Vi150 (^#) as indicated. The horizontal bracket indicates the region of L1 in which all three vasoinhibins display similar RMSF values (residues 47 to 60). (d) Dynamic changes of the secondary structure profile per residue of Vi150, Vi123, and Vi79 throughout 20 ns of MD simulation. Average composition of at least 3 independent MD simulations. (e) Representative structures of Vi150, Vi123, and Vi79 at the end of the 20 ns MD simulation. Structural motifs are indicated.