Literature DB >> 16901474

Progesterone binding to the tryptophan residues of human alpha1-acid glycoprotein.

J R Albani1.   

Abstract

Binding studies between progesterone and alpha1-acid glycoprotein allowed us to demonstrate that the binding site of progesterone contains one hydrophobic tryptophan residue and that the structure of the protein is not altered upon binding. The data obtained at saturated concentrations of progesterone clearly reveal the type of interaction at physiological levels.

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Year:  2006        PMID: 16901474     DOI: 10.1016/j.carres.2006.07.012

Source DB:  PubMed          Journal:  Carbohydr Res        ISSN: 0008-6215            Impact factor:   2.104


  4 in total

1.  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.

Authors:  Daniel Kmiecik; Jihad René Albani
Journal:  J Fluoresc       Date:  2010-03-30       Impact factor: 2.217

2.  Tunable recognition of the steroid alpha-face by adjacent pi-electron density.

Authors:  T Friscić; R W Lancaster; L Fábián; P G Karamertzanis
Journal:  Proc Natl Acad Sci U S A       Date:  2010-07-12       Impact factor: 11.205

3.  Relation between proteins tertiary structure, tryptophan fluorescence lifetimes and tryptophan S(o)→(1)L(b) and S(o)→(1)L(a) transitions. Studies on α1-acid glycoprotein and β-lactoglobulin.

Authors:  Jihad René Albani
Journal:  J Fluoresc       Date:  2011-02-01       Impact factor: 2.217

4.  New insights in the interpretation of tryptophan fluorescence : origin of the fluorescence lifetime and characterization of a new fluorescence parameter in proteins: the emission to excitation ratio.

Authors:  J R Albani
Journal:  J Fluoresc       Date:  2007-04-26       Impact factor: 2.525

  4 in total

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