[en] Computer simulation is used for comparative investigation of the molecular dynamics of rhodopsin containing the chromophore group (11-cis-retinal) and free opsin. Molecular dynamics is traced within a time interval of 3000 ps; 3 × 10⁶ discrete conformational states of rhodopsin and opsin are obtained and analyzed. It is demonstrated that the presence of the chromophore group in the chromophore center of opsin influences considerably the nearest protein environment of 11-cis-retinal both in the region of the β-ionone ring and in the region of the protonated Schiff base bond. Based on simulation results, a possible intramolecular mechanism of keeping rhodopsin as a G-protein-coupled receptor in the inactive state, i.e., the chromophore function as an efficient ligand antagonist, is discussed.