ИСТИНА

The visual pigment rhodopsin possesses unique properties: spectral tuning (naturally there are a lot of various visual pigments, absorbing light in a wide range of spectrum from 350 up to 650 nm, but the only one photosensitive element – 11-cis-retinal inserted into different matrices – could provide such a tremendous amount of different light sensors); a unique speed of a photochemical reaction of chromophore isomerisation (about of 80 fs) and quantum yield (0,65); dark state regeneration (ability to form a pigment-protein complex very quickly and without any involvement of enzymes or catalysing components). The properties of the rhodopsin molecule as a light-sensitive receptor have to be defined by a specific interaction of the 11-cis-retinal group with protein surrounding in a chromophore binding pocket. The understanding of the rhodopsin’ spectral and photochemical properties, as well as its important physiological feature – a non-ability to bind G-protein in a dark state, it is extremely necessary to know the details of the 11-cis-retinal conformational position and amino acid residues of the chromophore center and their mutual interaction. The rhodopsin native conformational behaviour has been compared and analyzed with the mutant version one, which is associated with the origin of a disease of retinitis pigmentosa. In the MD simulation studies some peculiarities of the conformational state of rhodopsin and its chromophore group, 11-cis-retinal chromophore, have been enlightened. Knowledge of details of the rhodopsin dark-adapted state has also to be important from the point of view of new fundamental results on the molecular mechanism of super-fast reactions in the visual pigment of photoreceptor cells as well as from the applied point of view – the design of new bioelectronic and photoelectronic systems.