NDLI: Energy Transfer Studies between Trp Residues of Three Lipocalin Proteins Family, α$_{1}$-Acid Glycoprotein, (Orosomucoid), β-Lactoglobulin and Porcine Odorant Binding Protein and the Fluorescent Probe, 1-Aminoanthracene (1-AMA)

Content Provider	SpringerLink
Author	Albani, Jihad R. Bretesche, Loïc Vogelaer, Julie Kmiecik, Daniel
Copyright Year	2015
Abstract	Energy transfer studies between Trp residues of α$_{1}$-acid glycoprotein, β-lactoglobulin and porcine odorant binding protein (OBP) and the fluorescent probe 1-aminoanthracene (1-AMA) were performed. 1-AMA binds to the hydrophobic binding sites of the three proteins inducing a decrease in the fluorescence intensity of the Trp residues accompanied by an increase of that of 1-AMA. Our results indicate that 1-AMA is in close contact with hydrophobic tryptophan residue of β-lactoglobulin (Trp 19) to the difference of its binding to OBP, where Trp residues are far from the pocket and to α$_{1}$-acid glycoprotein where three Trp residues are present at different areas of the protein.
Starting Page	167
Ending Page	172
Page Count	6
File Format	PDF
ISSN	10530509
Journal	Journal of Fluorescence
Volume Number	25
Issue Number	1
e-ISSN	15734994
Language	English
Publisher	Springer US
Publisher Date	2015-01-18
Publisher Place	Boston
Access Restriction	Subscribed
Subject Keyword	α$_{1}$-acid glycoprotein β-Lactoglobulin Porcine odorant binding protein (OBP) Tryptophan 1- Aminoanthracene (1-AMA) Förster energy transfer Biomedicine general Biophysics and Biological Physics Biotechnology Biochemistry Analytical Chemistry
Content Type	Text
Resource Type	Article
Subject	Clinical Biochemistry Sociology and Political Science Biochemistry Clinical Psychology Spectroscopy Law

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Energy Transfer Studies between Trp Residues of Three Lipocalin Proteins Family, α$_{1}$-Acid Glycoprotein, (Orosomucoid), β-Lactoglobulin and Porcine Odorant Binding Protein and the Fluorescent Probe, 1-Aminoanthracene (1-AMA)