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

. 2020 Feb 14;10:2657. doi: 10.1038/s41598-020-59583-2

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

© The Author(s) 2020

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/.

PMC Copyright notice

(a) Localized structural fluctuation (LSF) network of interactions from a MD simulation of P23H rhodopsin in the dark, inactive-state. In the network representation of the LSFs the nodes represent C-α amino acid residues and the links between the nodes represent localized interactions. In the network representation of the LSF, we find that the connections in the inactive receptor are grouped into three separate communities. (b) The corresponding LSF is mapped onto a 3-D cartoon representation of P23H rhodopsin. (c) Overlay ribbon diagram representation of the extracellular (EC) backbone of dark-state WT rhodopsin (gray, transparent) and P23H rhodopsin (gray). A ball-and-stick representation of WT (transparent) and P23H (CPK coloring) residues Cys110 and Cys187 are also displayed showing the ruptured bond in P23H when compared with the WT receptor. Free energy surfaces derived from the full correlation analyses (FCA) of the MD trajectories of (d) WT and (e) P23H rhodopsin. The C-α representation of the rhodopsin molecules illustrate the dominant motion within the minimum of the energy surfaces where regions colored in red show greater mobility and regions in blue have less mobility.