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. 2019 Oct 1;9:14128. doi: 10.1038/s41598-019-49912-5

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© The Author(s) 2019

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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NMR derived secondary structure and topology of hPIRT. (a) The light blue (gray) colored circles indicate NMR assigned (unassigned) residues. (b) The TROSY-HSQC of hPIRT reconstituted in DPC shows a relatively well-resolved spectrum with dispersion consistent with a α-helical membrane protein. (c) The plot of the consensus TALOS-N predicted hPIRT secondary structure derived from experimental hPIRT Cα, C_β, and C′ chemical shifts. Red, black, and blue bars indicate the probability of α-helix, loop, and β-sheet respectively. (d) Solvent paramagnetic enhancement in spin relaxation, ε, from Gd(III)-DTPA confirm the hydrophobic nature of the two transmembrane α-helices and the amphipathic nature of the C-terminal α-helix. Larger magnitude values of ε are consistent with solvent accessibility and small magnitude ε values are suggestive of protection from Gd(III)-DTPA relaxation enhancement by the membrane mimic. These results indicate that hPIRT has a relatively unstructured N-terminus, two transmembrane helices, and an amphipathic C-terminal α-helix.