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. 2017 Jul 31;7:6864. doi: 10.1038/s41598-017-07250-4

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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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Spatial structure of TLR4-TMICL. (A) NMR-derived spatial structure of TLR4-TMICL in DMPG/DHPC q = 0.4 bicelles, pH 6.0, LPR 200. Residues in the hydrophobic part of the ICL region of the protein are indicated and painted according to their physical properties: Hydrophobic by orange, aromatic by yellow, polar by green and positively charged – by blue. (B) relative rates of the amide protons exchange with the solvent, as measured in the CLEANEX experiment²⁶ for the TLR4-TMICL in DMPG/DHPC q = 0.4 bicelles at pH 7.2. (C) Dependence of the Hε1 chemical shift of H657 on the ambient pH which was used to determine the corresponding pKa. The fit of the obtained data to the equation (1) is shown by the red solid line.