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. 2020 Mar 4;6(10):eaay7505. doi: 10.1126/sciadv.aay7505

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Copyright © 2020 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works. Distributed under a Creative Commons Attribution License 4.0 (CC BY).

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Fig. 6 — The sequences of 468 rhodopsins were aligned and analyzed to compare the evolutionary rates of residues within each TM domain. (A) The evolutionary rates associated with each residue within TM2 were converted into conservation scores and mapped onto a structural model of rhodopsin. (B) The evolutionary rates associated with each residue within TM7 were converted into conservation scores and mapped onto a structural model of rhodopsin. (C) The conservation scores associated with the surface (closed circles) and buried (open circles) residues within all of the TM domains of rhodopsin (gray) are compared to those within TMs 2 (blue) and 7 (red), specifically. The average conservation score associated with each distribution is plotted, along with whiskers showing the standard error plotted for reference.