[Determination of the accessibility and localization of tryptophan residues in the influenza virus hemagglutinin molecule].
The accessibility and localization of tryptophane residues in the influenza viral hemagglutinin molecule have been determined by measuring specific quenching of tryptophane fluorescence by neutral (acrylamide), anionic (I-) and cationic (Cs+) quenchers. It has been shown that acrylamide quenches 64% of tryptophane fluorescence in H3-hemagglutinin whereas I- and Cs+ quench only 34%. The tryptophanyl residues have been assumed to be located in the hemagglutinin molecule both in the cationic and anionic environments. 64% of tryptophanyls have been shown to be located on the surface of the protein globule.
D000818:Animals; D002642:Chick Embryo; D005453:Fluorescence; D006389:Hemagglutinins, Viral / Q000032:analysis*; D009980:Influenza A virus / Q000032:analysis / Q000276:immunology*; D014364:Tryptophan / Q000032:analysis*
D006389:Hemagglutinins, Viral; D014364:Tryptophan
Opredelenie dostupnosti i lokalizatsii ostatkov triptofana v molekule gemaggliutinina virusa grippa.