Motions studies of the human α1-acid glycoprotein (orosomucoid) followed by red-edge excitation spectra and polarization of 2-p-toluidinylnaphthalene-6-sulfonate (TNS) and of tryptophan residues
Author:
Publisher
Elsevier BV
Subject
Organic Chemistry,Biochemistry,Biophysics
Reference22 articles.
1. Measurement of subnanosecond anisotropy decays of protein fluorescence using frequency-domain fluorometry.
2. Red-edge excitation of fluorescence and dynamic properties of proteins and membranes
3. Fluorescence anisotropy decay studies upon hemoglobin A and its subunits
4. Quenching of protein fluorescence by oxygen. Detection of structural fluctuations in proteins on the nanosecond time scale
5. Proof of nanosecond timescale relaxation in apomyoglobin by phase fluorometry
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1. Energy Transfer Studies between Trp Residues of Three Lipocalin Proteins Family, α1-Acid Glycoprotein, (Orosomucoid), β-Lactoglobulin and Porcine Odorant Binding Protein and the Fluorescent Probe, 1-Aminoanthracene (1-AMA);Journal of Fluorescence;2015-01
2. Tryptophan 19 residue is the origin of bovine β-lactoglobulin fluorescence;Journal of Pharmaceutical and Biomedical Analysis;2014-03
3. Relation Between Proteins Tertiary Structure, Tryptophan Fluorescence Lifetimes and Tryptophan So → 1Lb and So → 1La Transitions. Studies on α1-acid Glycoprotein and β-lactoglobulin;Journal of Fluorescence;2011-02-01
4. Fluorescence properties of porcine odorant binding protein Trp 16 residue;Journal of Luminescence;2010-11
5. Effect of 1-Aminoanthracene (1-AMA) Binding on the Structure of Three Lipocalin Proteins, the Dimeric β Lactoglobulin, the Dimeric Odorant Binding Protein and the Monomeric α1-Acid Glycoprotein. Fluorescence Spectra and Lifetimes Studies;Journal of Fluorescence;2010-03-30
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