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. 2019 Dec 30;9:20332. doi: 10.1038/s41598-019-56993-9

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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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CIU plots of monomeric (a,c,e) and dimeric (b,d,f) species of the constructs V_C1, V_C1_C2, and FL_RAGE. The monomeric species of V_C1 (+8; m/z range 2290–2291) and V_C1_C2 (+11; m/z range 3174.3–3175.3) did not show unfolding in this energy range, while the dimeric species showed unfolding at 375 eV (+13; m/z range 3522–3523) and 1750 eV (+17; m/z range 4113–4115), respectively. FL_RAGE exhibited unfolding at 1375 eV for the monomer (+13; m/z range 3215–3217) and 2250 eV for the dimer (+18; m/z range 4642–4644). The relatively higher ion energy necessary for the unfolding of V_C1_C2 and FL_RAGE as compared to V_C1 indicates a stabilizing effect of the C2 and TM domain in the protein.