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. 2017 Jun 6;7:2835. doi: 10.1038/s41598-017-03013-3

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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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The VV mutation reduces structural flexibility of the VAMP2 TMD. (a) Sequences and space-filling models of the transmembrane domain of the WT and VV mutant VAMP2 as an α-helix. Yellow designates sulphur, green carbon, white hydrogen and red oxygen. Arrows designate positions of G₁₀₀ and C₁₀₃, arrowheads point to the volume changes in the mutated sites. (b) ATR–IR spectra of the synthetic peptide VAMP2_95-116 (WT or VV mutant) in a lipid multi-bilayer (DOPC) were obtained at a peptide/lipid ratio of 1/20 at room temperature. After 1 h peptides were diluted with DOPC to a peptide/lipid ratio of 1/250 and structural changes measured for 2 h at room temperature. The ratios of α-helices vs β-sheets are given for wild-type (○) or the VV mutant (●). The curves were obtained fitting exponential growth. The time constants (τ) are given next to the curves.