Localization of light-induced conformational changes in bovine rhodopsin.
Conformational changes in the extradiscal regions of rhodopsin induced by illumination were investigated by modifying the visual pigment by mild treatment with cyanogen bromide prior to and after light exposure. Light induced an increased yield of cleavage of the Met bond 253-254 and a new cleavage at the Met bond 155-156 of the rhodopsin polypeptide chain. These residues, located at the beginnings of the membrane-buried helices 6 and 4, respectively, were concluded to become extradiscally exposed upon illumination.
Pellicone
C
C
Nullans
G
G
Virmaux
N
N
D000818:Animals; D002417:Cattle; D003488:Cyanogen Bromide / Q000494:pharmacology; D004591:Electrophoresis, Polyacrylamide Gel; D005136:Eye Proteins / Q000032:analysis; D008027:Light; D011487:Protein Conformation; D012168:Retinal Pigments / Q000032:analysis*; D012243:Rhodopsin / Q000032:analysis*; D012374:Rod Cell Outer Segment / Q000032:analysis; D017299:Rod Opsins; D013053:Spectrophotometry
D005136:Eye Proteins; D012168:Retinal Pigments; D017299:Rod Opsins; D012243:Rhodopsin; D003488:Cyanogen Bromide