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. 2022 Dec 6;13:7508. doi: 10.1038/s41467-022-35279-1

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© The Author(s) 2022

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. 2 — A Schematic representation of peptide (top panel) and ester bonds (bottom panel). (B, C) Effect of replacing backbone amides with ester oxygens at positions lining S_ext and S_cen in bCLC-k (B) and CLC-0 (C) on P_Br (black bars), P_NO3 (red bars) and P_I (green bars). Nomenclature of α-hydroxy acid substitutions is explained in Methods. Data are Mean ± St.Dev. of n > 4 repeats from N ≥ 3 independent oocyte batches, individual data points are shown as cyan circles. The statistical significance of the effects of the mutants on the permeability ratios of each ion (indicated by *) was evaluated with a one-sided Student’s t-test with a Bonferroni correction (see “Methods”). Mean values and p values are reported in Supplementary Table 1. Individual data points are shown grouped by ion in Supplementary Fig. 5. Raw data for B, C is included in the Source Data Files.