[Study of the equilibrium dynamics of cell protein structure using the tryptophan fluorescence method at room temperature].
Room-temperature tryptophane phosphorescence (RTTP) of liver tissue cells has been studied. It is shown that over a millisecond range RTTP is absent in soluble proteins of the cytoplasm, karyoplasm, mitochondrial matrix, and the phosphorescent signal is controlled only by proteins of the subcellular structures incorporated into the membranes. It is concluded that, unlike the membrane proteins, the cytoplasm and organelle matrix-soluble proteins are characterized by a high level of intramolecular equilibrium mobility, which causes RTTP quenching following a dynamic mechanism. In membrane proteins, which fluoresce in a millisecond range the level of equilibrium conformation motions is limited, probably, due to protein-protein and protein-lipid interactions.
D000818:Animals; D002467:Cell Nucleus / Q000032:analysis; D005453:Fluorescence; D008099:Liver / Q000032:analysis* / Q000648:ultrastructure; D008565:Membrane Proteins / Q000032:analysis; D008930:Mitochondria, Liver / Q000032:analysis; D011487:Protein Conformation; D011506:Proteins / Q000032:analysis*; D051381:Rats; D013696:Temperature; D014364:Tryptophan / Q000032:analysis*
D008565:Membrane Proteins; D011506:Proteins; D014364:Tryptophan
Issledovanie ravnovesnoĭ dinamiki struktury belkov kletki metodom triptofanovoĭ fosforestsentsii pri komnatnoĭ temperature.