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. Author manuscript; available in PMC: 2017 Jul 7.
Published in final edited form as: Biochemistry. 2017 Apr 21;56(17):2338–2348. doi: 10.1021/acs.biochem.7b00165

Figure 4.

Figure 4

Dimer interface analysis of dark and bleached states of green opsin. Panels A–C show side views of the green dimer in the dark and bleached states. Panels D and E show bottom and top views of the green dimer in the dark and bleached states, respectively. In all panels, the dimer in the dark state is shown on the left while the dimer in the bleached state is shown on the right. One monomer is displayed in a cartoon representation and the second monomer as a surface. Both the cartoon and surface representations show the dimer interface color-coded according to H/D exchange as follows: dark blue for 0–4%, light blue for 5–9%, cyan for 10–14%, cadet blue for 15–19%, green for 20–24%, light green for 25–29%, yellow for 30–34%, orange for 35–39%, and red for 40–44%. Undefined regions are colored gray.