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Computer simulation was used to perform a comparative study of the molecular dynamics of rhodopsin containing the chromophore group (11-cis-retinal) and free opsin. The molecular dynamics were followed over a time interval of 3000 psec; a total of 3 x 10(6) discrete conformational states of rhodopsin and opsin. The presence of the chromophore group in the chromophore center of opsin was shown to have significant effects on the immediate protein environment of the chromophore and the conformational state of the cytoplasmic domain, but to have virtually no effect on the conformational state of the intradisk domain. The simulation results are used to discuss the possible intramolecular mechanism by which rhodopsin is maintained as a G-protein-coupled receptor in the inactive state, i.e., the function of the chromophore as an effective antagonist ligand.

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