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. 2018 Mar 16;8:4664. doi: 10.1038/s41598-018-22959-6

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© The Author(s) 2018

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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hCFTR^TS conformational changes when both AMPPNP and Kalydeco were bound. (A) HDX perturbation data mapped to the cryo-EM structure (PDB 5UAK). As shown in the key, a color gradient is used to represent the average deuterium uptake differences across all 6 time points between the apo and ligand bound states of hCFTR^TS. White indicates regions that were not detected for every replicate at every time point in the HDX experiments. The ICL4 region was zoomed in to show the protected peptides. F₅₀₈ was highlighted in red and represented as sticks. (B) Deuterium uptake time-course curves of the TMD2 peptide which showed protection upon ligand binding. Data represent the means ± SD (n = 2–3). Charge state of the peptide ion is also noted.