Förster energy-transfer studies between Trp residues of alpha1-acid glycoprotein (orosomucoid) and the glycosylation site of the protein.
Energy-transfer studies between Trp residues of alpha(1)-acid glycoprotein and the fluorescent probe Calcofluor White were performed. Calcofluor White interacts with carbohydrate residues of the protein, while the three Trp residues are located at the surface (Trp-160) and in hydrophobic domains of the protein (Trp-25 and Trp-122). Binding of Calcofluor to the protein induces a decrease in the fluorescence intensity of the Trp residues accompanied by an increase of that of Calcofluor White. Efficiency (E) of Trp fluorescence quenching was determined to be equal to 45%, and the Förster distance R(o), at which the efficiency of energy transfer is 50%, was calculated to be 18.13 A. This low distance and the value of the efficiency clearly indicate that energy transfer between Trp residues and Calcofluor White is weak.
Albani
Jihad R
JR
Laboratoire de Biophysique Moléculaire, Université des Sciences et Technologies de Lille, Bâtiment C6, 59655 Villeneuve d'Ascq, France. jihad-rene.albani@univ-lille1.fr
D001557:Benzenesulfonates; D031541:Fluorescence Resonance Energy Transfer; D005456:Fluorescent Dyes; D006031:Glycosylation; D007700:Kinetics; D009961:Orosomucoid / Q000737:chemistry*; D014364:Tryptophan / Q000737:chemistry*
D001557:Benzenesulfonates; D005456:Fluorescent Dyes; D009961:Orosomucoid; C007061:C.I. Fluorescent Brightening Agent 28; D014364:Tryptophan