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. 2017 Sep 5;7:10419. doi: 10.1038/s41598-017-10571-z

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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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% DFI profile of WT hBChE and pentavalent mutant. (a) The % DFI profiles of WT BChE (blue) and BChE_V4 (x-axis – residue numbers, y-axis – % DFI values at each position). (b) Color-coded structure diagrams depicting the % DFI values at each position. The circled regions are part of the monomer-monomer contact region (V377, D378, T457, K458, A459, I462, Y500, R509, M511, T512, K513, R514, L515). (c) The % DFI profiles of monomeric (blue) and dimeric (green) WT BChE. (d) The % DFI profiles of monomeric (red) and dimeric (purple) BChE_V4. (e) Color-coded structure diagrams depicting the values of % DFI differences between the dimeric forms of WT BChE and BChE_V4 at each position. The red-white-blue code reveals loci with increased flexibility (shades of red), decreased flexibility (shades of blue) or no change (white) in the mutant dimer vs. the WT dimer.