Characterization of a deswapped triple mutant bovine odorant binding protein

• Published in: International journal of molecular sciences Vol. 12; no. 4; pp. 2294 - 2314
• Main Authors: Polverini, Eugenia, Lardi, Paolo, Mazzini, Alberto, Sorbi, Robert T, Virna, Conti, Ramoni, Roberto, Favilla, Roberto
• Format: Journal Article
• Language: English
• Published: Switzerland MDPI AG 01-04-2011; Molecular Diversity Preservation International (MDPI)
• Subjects: Animals; Anthracenes - chemistry; Cattle; Fluorescence Resonance Energy Transfer; Hydrogen-Ion Concentration; Ligands; molecular dynamics; Molecular Dynamics Simulation; Mutagenesis; odorant binding proteins; Protein Denaturation; Protein Folding; Protein Structure, Secondary; Protein Structure, Tertiary; Proteins; Receptors, Odorant - chemistry; Receptors, Odorant - genetics; Receptors, Odorant - metabolism; Signal transduction; Swine; unfolding/refolding; Italy; molecular dynamics; odorant binding proteins; unfolding/refolding
• ISSN: 1422-0067; 1661-6596; 1422-0067
• DOI: 10.3390/ijms12042294

The stability and functionality of GCC-bOBP, a monomeric triple mutant of bovine odorant binding protein, was investigated, in the presence of denaturant and in acidic pH conditions, by both protein and 1-aminoanthracene ligand fluorescence measurements, and compared to that of both bovine and porcine wild type homologues. Complete reversibility of unfolding was observed, though refolding was characterized by hysteresis. Molecular dynamics simulations, performed to detect possible structural changes of the monomeric scaffold related to the presence of the ligand, pointed out the stability of the β-barrel lipocalin scaffold.