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. 2017 Dec 8;7:17229. doi: 10.1038/s41598-017-17396-w

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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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Mobility parameter ΔH₀ ⁻¹ profiles of the C-terminal helical bundle. The mobility parameter ΔH₀ ⁻¹ was obtained in the closed (black) and open (red) configuration of MscL. The spin-labelled mutant channels were opened by applying 25 mol% LPC to liposomes reconstituted with the mutant proteins, as previously reported^6,20. Except for the first ten amino acid residues (A110 through E119) showing higher mobility in the open channel configuration compared to the closed channel, the profiles are almost identical showing no difference in the mobility of the remaining 17 residues (V120 through S136) between the closed and the open MscL channel.