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. 2023 Aug 12;23:399. doi: 10.1186/s12872-023-03417-2

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© The Author(s) 2023

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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.

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Fig. 2 — (A) The illustration indicated the amino acid changes in KCNQ1 found in our study. (B) KCNQ1 p.Leu250Pro was located in a highly conserved region across all available species evolutionally (upper). Altered secondary structure of p.Leu250Pro mutant protein was predicted when compared with the wild type (the altered residue was shown with red arrow) (lower). (C) KCNQ1 p.Arg555Cys was also located in a highly conserved region across all available species evolutionally (upper). No significant alteration of the secondary structure of p.Arg555Cys mutant protein was predicted when compared with the wild type (lower, the altered residue is shown with red arrow) (lower)