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. 2019 Jan 28;9:800. doi: 10.1038/s41598-018-37280-5

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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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In silico study of the impact of K35E over the structural stability of human IL-2. Root mean square deviation (RMSD) of heavy atoms of IL-2 (black line) and K35E variant (red line) over a 200 ns molecular dynamics (MD) simulation are shown in (a). Root mean square fluctuation (RMSF) per residue along the primary sequence of IL-2 (black line) and K35E variant (red line) are shown in (b). Panels c and d show the structural superposition of the initial (0 ns, blue) and final (200 ns, red) structures from the MD simulations using the mutated and non-mutated proteins respectively. The arrow indicates the bending on the N-terminal segment in the K35E-containing variant, while the circle encloses the replacement at position 35.