Abstract
Rhodopsin is the G-protein-coupled receptor (GPCR) responsible for scotopic vision in vertebrates. Although published X-ray structures are similar, the conformation and orientation of the retinal chromophore of active rhodopsin are not established unambiguously. Under debate is a proposed flip of all-trans retinal in the active state, due to a change of the roll angle of the β-ionone ring, as well as the central part of the polyene chain that includes the C9-Me group [1]. Here we applied solid-state 2H NMR spectroscopy to study the structure and orientation of the retinylidene ligand in the active state of rhodopsin in aligned membranes [2].
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