Models of ionic transport in biological membranes. Raman spectroscopy as a probe of valinomycin, gramicidin A', and rhodopsin conformations.
There is evidence that membrane proteins can serve as the functional units of ionic transport in biological membranes. Laser Raman spectroscopy has been used to probe specific molecular interactions inside two models of transport membrane proteins, valinomycin and gramicidin A. Conformational changes of these molecules, as well as specific interactions with ions, can be detected and may help elucidate how membrane transport proteins such as Na+ minus K+ ATPase and rhodopsin function. Resonance Raman spectroscopy has also been used to study conformational changes and protein-chromophore interactions in rhodopsin, the membrane protein that acts as the primary unit of visual excitation in the eye.
D000251:Adenosine Triphosphatases / Q000378:metabolism; D001693:Biological Transport, Active; D002462:Cell Membrane / Q000378:metabolism* / Q000502:physiology; D055598:Chemical Phenomena; D002621:Chemistry; D003201:Computers; D006096:Gramicidin; D007477:Ions / Q000378:metabolism*; D007834:Lasers; D008954:Models, Biological; D010786:Photoreceptor Cells / Q000648:ultrastructure; D011188:Potassium / Q000378:metabolism; D014176:Protein Biosynthesis; D011487:Protein Conformation; D012168:Retinal Pigments; D012243:Rhodopsin; D012964:Sodium / Q000378:metabolism; D013055:Spectrophotometry, Infrared; D013057:Spectrum Analysis / Q000379:methods; D014634:Valinomycin
D007477:Ions; D012168:Retinal Pigments; D006096:Gramicidin; D014634:Valinomycin; D012243:Rhodopsin; D012964:Sodium; D000251:Adenosine Triphosphatases; D011188:Potassium