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. 2017 Dec 7;7:17159. doi: 10.1038/s41598-017-17144-0

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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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FTIR spectroscopy of wild-type and alanine mutants of C55. Comparison of FTIR spectra of wild-type C55 (A) reconstituted into membrane bilayers with spectra of the C55 protein containing alanine mutations at (B) DAE, (C) FRH, (D) DSG, (E) YEV, (F) HHQ, (G) K, (H) LVFF, and (I) EDV. The bilayers were formed with dimyristoylphosphocholine (DMPC) and dimyristoylphosphoglycerol (DMPG) in a molar ratio of 10:3. The molar ratio of C55:total lipid was 1:50.