Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2024 May 23;57:31. doi: 10.1186/s40659-024-00501-5

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

© The Author(s) 2024

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.

PMC Copyright notice

Fig. 4 — Distance and angle variations between the transmembrane domains of the mutant protomers compared with the wild-type Cx50 protomer. Graphs show the distance (top two rows) and the angle (bottom 3 rows) between transmembrane domains in Cx50, Cx50R33E, Cx50E162R, Cx50E162Q and Cx50R33E,E162R protomers. The distance between TM1 and TM3 was measured between amino acid residues 25 and 159, and that between TM2 and TM4 was measured between amino acid residues 85 and 220. The inclination of TM2, TM3 and TM4 with respect to TM1 was calculated by finding the best fitted straight line passing through the C_α of all amino acid residues in each transmembrane domain. The results are presented as box plots (mean ± S.D.) for each protomer (A‒F) using the measurement from all frames from all three replicas. The outliers are presented as empty circles. The horizontal dashed line corresponds to the average for all six protomers for each construct and the gray shade corresponds to the standard deviation. Asterisks indicate a significant difference vs. the corresponding monomer in wild-type Cx50 using Kruskal–Wallis test (p < 0.05)