A proposed model for rhodopsin in photoreceptor membranes.
Transient electric birefringence studies have been made on bovine rhodopsin solubilized in the detergent lauryldimethylamine oxide from glutaraldehyde fixed rod outer segment (ROS) membranes. It was found that fixation caused no appreciable differences in the measured relaxation times when compared with unfixed ROS. On the basis of these findings a model for the orientation of rhodopsin in photoreceptor membranes is proposed which accounts for translational diffusion and two modes of rotational diffusion. The proposed model is related to a number of experimentally determined biophysical properties reported in the literature.
D008565:Membrane Proteins; D008954:Models, Biological; D010786:Photoreceptor Cells; D011487:Protein Conformation; D012168:Retinal Pigments; D012243:Rhodopsin
D008565:Membrane Proteins; D012168:Retinal Pigments; D012243:Rhodopsin