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. 2017 Sep 12;7:11361. doi: 10.1038/s41598-017-11625-y

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© The Author(s) 2017

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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Correlation between surface electrostatic charge and polymerase activity. (a) Structural model of the PB2 C-terminal was predicted by the web-server Geno3D and visualized with Chimera. The protein surface was presented from PB2 residues 700 to 703 (left). Coulomb’s law was applied to estimate the electrostatic potential, in which blue and red color indicated positively and negatively charged surface respectively. A change in surface electrostatic charge were observed with PB2-701 or PB2-702 mutation (middle and right). Correlation analyses were performed between overall surface charge of the PB2-700 to 703 region and polymerase activities in (b) 293T cells and (c) DF-1 cells at 37 °C. Overall surface charge, in the unit of kT/e, was defined as the sum of the charges from residues 700 to 703 determined by Coulomb’s law.