Investigation of membrane structure using fluorescence quenching by spin-labels. A review of recent studies.
Fluorescence quenching is the loss of fluorescence intensity which is observed when a fluorescent molecule or group interacts with another molecule or group, called the quencher. By use of tryptophan residues of proteins, together with specific probe molecules, quenching can be applied to problems of biological and model membrane structure. Quenching interactions are short range (less than 50 A) so that structure on the scale of molecular dimensions can be examined. This review summarizes the recent applications of fluorescence quenching by spin (nitroxide)-labeled molecules to problems of membrane structure, including determination of the distance of membrane-bound molecules from the membrane surface, the strength of lipid-protein interactions and the strength of protein-protein interactions within membranes. The unique advantages and the limitations of this powerful method are examined.
D000818:Animals; D002118:Calcium / Q000378:metabolism; D000252:Calcium-Transporting ATPases / Q000378:metabolism; D002151:Calorimetry; D002462:Cell Membrane / Q000648:ultrastructure*; D004578:Electron Spin Resonance Spectroscopy / Q000379:methods; D005456:Fluorescent Dyes; D006863:Hydrogen-Ion Concentration; D008563:Membrane Lipids / Q000032:analysis; D008565:Membrane Proteins / Q000032:analysis; D013113:Spin Labels; D013696:Temperature
D005456:Fluorescent Dyes; D008563:Membrane Lipids; D008565:Membrane Proteins; D013113:Spin Labels; D000252:Calcium-Transporting ATPases; D002118:Calcium