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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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Secondary structure and dynamics of TLR4-TMICL. (A) Secondary chemical shifts of Cα nuclei of TLR4-TMICL in the environment of DPC micelles (blue bars), DMPC/DHPC q = 0.4 bicelles (red bars) and DMPG/DHPC q = 0.4 bicelles (yellow bars). Positive values indicate the helical conformation. (B) Propensity of helical secondary structure for the residues of TLR4-TMICL in DMPG/DHPC bicelles, according to the chemical shift based prediction by TALOS-N⁵². (C) Correlation time of rotational diffusion measured for the individual amide groups of TLR4-TMICL in DMPG/DHPC q = 0.4 bicelles (red bars) and DPC micelles (blue bars). Correlation times were measured from the rates of cross-correlated relaxation⁵⁵. (D) Cross-peak intensities in the 3D HNCO spectrum of TLR4-TMICL in DMPG/DHPC q = 0.4 bicelles, expressed in relative units. Low intensity indicates the line broadening, enhanced transverse relaxation and motions in us-ms timescale. On top, the predicted TM domain (according to UniProt) and hydrophobic part of the ICL region (HR domain), homologous to the reported in ref. 23 are indicated.