[Phosphorescent analysis of the action of detergents on the internal dynamics of membrane proteins of human erythrocytes].
The slow (millisecond) internal dynamics of proteins isolated from human erythrocyte membranes under the action of ionic and nonionic detergents: sodium dodecyl sulfate (0.1-6 mM), sodium deoxycholate (0.16-6 MM), N-Lauroylsarcosine Na+-salt (Sarkosyl) (0.17-6 mM), digitonin (0.025-6 MM), and Tween-20 (0.01-6 mM) has been studied by the method of room-temperature tryptophan phosphorescence. It has been established that the destruction of protein ensembles, the disturbance of protein-lipid interactions, and the unfolding of proteins in membrane result in a considerable increase of slow intramolecular dynamics of proteins. The effects of detergents on the structural and dynamical state of membrane proteins differ depending on their chemical features. On the bases of the results obtained, it has been concluded that the low internal dynamics of membrane proteins in situ, compared with most soluble proteins, is due to the presence of protein ensembles in membrane, the isolation of macromolecules from the aqueous surroundings by the lipid bilayer, and a high content of alpha-helices and beta-sheets in macromolecules.
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D003902:Detergents / Q000737:chemistry*; D004910:Erythrocyte Membrane / Q000737:chemistry*; D006801:Humans; D008051:Lipid Bilayers / Q000737:chemistry*; D008163:Luminescent Measurements / Q000379:methods; D008565:Membrane Proteins / Q000737:chemistry*; D020836:Protein Structure, Quaternary; D017433:Protein Structure, Secondary
D003902:Detergents; D008051:Lipid Bilayers; D008565:Membrane Proteins