Interactions of new lactoglobulin variants with tetracaine: crystallographic studies of ligand binding to lactoglobulin mutants possessing single substitution in the binding pocket

drug-protein interactions: binding of serotonin and arachidonyl serotonin to β-lactoglobulin

Interactions of β-lactoglobulin with Cationic Surfactants: Spectroscopy Study

The interactions of β-lactoglobulin AB in the presence of cationic surfactants such as Cetyltrimethylammonium bromide and Cetyltrimethylammonium p-Toluenesulfonate have been investigated using a variety of experimental techniques such as conductivity, UV-Vis spectrophotometry and fluorimetry. The conductivity of surfactants aqueous solutions with β-lactoglobulin shows that the cmc of cationic s...

Putative Binding Sites of Dopamine and Arachidonoyl Dopamine to Beta-lactoglobulin: A Molecular Docking and Molecular Dynamics Study

Because of participation in many aspects of human life, and due to oxidation-sensitive characteristics of dopamine (DA) and arachidonoyl dopamine (AA-DA), the necessity of biocompatible carrier to keep them against oxidation is of importance. In this work, we explored the putative binding sites of DA and AA-DA to -lactoglobulin (BLG) as potent carrier. Docking results identified the binding si...

Biopolymer-surfactant Interactions: Binding Studies of Cetyltrimethyl Ammonium Bromide, Cetyl Pyridinium Bromide and Dodecyl Trimethyl Ammonium Bromide with Β-lactoglobulin

Binding studies of cationic detergents such as cetyltrimethyl ammonium bromide, Cetyl pyridinium bromide and dodecyl trimethyl ammonium bromide with β Lactoglobulin were carried out by equilibrium dialysis, ultraviolet difference and circular dichroism techniques at 25 C. Binding isotherms at pH 5·0, 7·0 and 9·0 show cooperative binding at all concentrations of detergents and the number of avai...

Temperature jump studies of the binding of bromphenol blue to beta-lactoglobulin in the vicinity of the N--R transition.

Several investigators have studied the equilibrium properties of &lactoglobulin over a wide range of pH (1-14). Below pH 3.5 the protein, which exists in the native state as a dimer of molecular weight 35,500, dissociates into two identical monomer units of molecular weight 17,750 (l-3). Between pH 3.5 and pH 5.2 tetramerization of the dimer units has been observed for the more common genetic v...