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. 2023 Jan 9;14:128. doi: 10.1038/s41467-023-35790-z

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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 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. 5 — a The mean effective coupling free energy from the matrices in Fig. 4 are mapped on the structure of GPCRs. The GPCR indices are provided for reference. Color bars are in units of kJ mol⁻¹. Regions of the protein colored in dark magenta represent strongly coupled residues while those in dark blue are not coupled. b Distribution of the fraction of strongly coupled residues (f_c) in GPCRs (n = 45). c Comparison of the mean fraction of strongly coupled residues in GPCRs (n = 45; 13.0 ± 4.5) and soluble proteins (SPs, n = 25; 15.7 ± 3.7). Data are presented as mean values ± one standard deviation. d Effective coupling free energies between transmembrane (TM) helices averaged over the 45 GPCRs. The mean standard deviations in 〈∆G_c $⟩$ are of the order of 4–6 kJ mol⁻¹, indicating significant variability. Despite this variability, TM3 turns out to be strongly coupled to every other TM helix. Source data are provided as a Source data file.