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. 2020 Dec 3;3:731. doi: 10.1038/s42003-020-01455-6

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© The Author(s) 2020

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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Fig. 3 — a Sequence of the NHE1-LID with indicated peptide regions corresponding to nLID_542-569 and cLID_567-592 and with Agadir prediction of helicity and helical wheel representations⁹⁴. The basic PI(4,5)P₂ Site II (blue) and hydrophobic motifs (HM1, HM2) (yellow) indicated above. b Far-UV CD spectra of nLID_542-569 alone and in the presence of various lipids and at two different pH values. c Far-UV CD spectra of cLID_567-592 alone and in the presence of various lipids. d Fluorescence emission spectra of nLID_542-569 alone and upon addition of POPC/POPS and POPC/POPS/PI(4,5)P₂ SUVs. e Center of spectral mass analysis of nLID_542-569 fluorescence emission spectra from a SUV titration series revealed an apparent membrane affinity of 0.8 mM for nLID_542-569.