[Localization of the tryptophan residues of influenza virus matrix protein in reconstructed proteoliposomes: a fluorescent analysis].
Influenza virus matrix protein (M-protein) interaction with model phospholipid membranes, liposomes, was studied. Measuring of the effectiveness of energy transfer from M-protein triptophan residues to a fluorescent zond pyren included into the lipid phase of proteoliposomes was employed to assess the steric organization of the proteoliposome protein-lipid complex. A steric model is proposed in which M-protein molecules are located on the surface of lipid bilayer forming trimers. Analysis of pyren fluorescence proper demonstrated a strong influence of M-protein on the lipid bilayer structure: the viscosity of the lipid phase in the presence of M-protein was increased 2.3-fold.
D004735:Energy Transfer; D005456:Fluorescent Dyes / Q000032:analysis; D008051:Lipid Bilayers / Q000032:analysis; D008081:Liposomes / Q000032:analysis*; D008958:Models, Molecular; D009975:Orthomyxoviridae / Q000032:analysis*; D011510:Proteolipids / Q000032:analysis*; D014364:Tryptophan / Q000032:analysis*; D014764:Viral Proteins / Q000032:analysis*; D014771:Virion / Q000032:analysis
D005456:Fluorescent Dyes; D008051:Lipid Bilayers; D008081:Liposomes; D011510:Proteolipids; D014764:Viral Proteins; C020485:proteoliposomes; D014364:Tryptophan
Lokalizatsiia ostatkov triptofana matriksnogo belka virusa grippa v rekonstruirovannykh proteoliposomakh: fliuorestsentnyĭ analiz.