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. Author manuscript; available in PMC: 2017 Jan 31.
Published in final edited form as: Nat Struct Mol Biol. 2011 Jan 30;18(3):392–394. doi: 10.1038/nsmb.1982

Figure 3.

Figure 3

2H NMR relaxation of retinal sheds new light on activation mechanism of rhodopsin. (a) Summary of analysis of solid-state 2H NMR measurements. Order parameters of rapidly spinning methyl groups are designated by SC3; the pre-exponential factor is k0 for 3-fold axial jumps or D0 for continuous diffusion; and Ea indicates the activation energy. (The diffusion model assumes either D=0 (right) or ηDD/D=1 (left) except for the C5-Me in Meta I, where ηD≠1.) (b–d) Proposed activation mechanism for rhodopsin in membranes based on X-ray19, FTIR11, and 2H NMR data12 (see text). Isomerization of retinal displaces the E2 loop towards the extracellular (e) side with fluctuations of TM helices H5 and H6 exposing transducin (Gt) recognition sites on the opposing cytoplasmic (c) surface. Figure produced (PDB code 1U19)3 using PyMOL [http://pymol.sourceforge.net/]