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Upon absorption of a photon, the bound 11-
cis-
retinoid isomerizes to the all-
trans
form resulting in a protein conformational change that enables it to activate its G protein, transducin, to begin the visualsignal transduction cascade. The native ligand, 11-
cis-
retinal, acts as an inverse agonist to both the apoproteins of rod and cone visual pigments (opsins); all-
trans-
retinal is an agonist. Truncated analogs of retinal have been used to characterize structure–function relationships with rodopsins, but little has been done with cone opsins. Activation of transducin by an opsin is one method to characterize theconformational state of the opsin. This chapter describes an in vitro transducin activation assay that can be used with coneopsins to determine the degree to which different ligands can act as an agonist or an inverse agonist to gain insight intothe ligand-binding pocket of cone opsins and differences between the different classes of opsins. The understanding of theeffects of ligands on cone opsin activity can potentially be applied to future therapeutic agents targeting opsins.