title: Characterization of a deswapped triple mutant bovine odorant binding protein.
abstract: 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.
authors: Department of Physics and CNISM, University of Parma, V.le Usberti 7A, Parma, Italy; E-Mails: eugenia.polverini@fis.unipr.it (E.P.); paololardi@libero.it (P.L.); alberto.mazzini@fis.unipr.it (A.M.); roberttibor.sorbi@fis.unipr.it (R.T.S.).
authors: Eugenia
authors: E
authors: Polverini
authors: Paolo
authors: P
authors: Lardi
authors: Alberto
authors: A
authors: Mazzini
authors: Robert T
authors: RT
authors: Sorbi
authors: Conti
authors: C
authors: Virna
authors: Roberto
authors: R
authors: Ramoni
authors: Roberto
authors: R
authors: Favilla
mesh_terms: D000818:Animals; D000873:Anthracenes / Q000737:chemistry; D002417:Cattle; D031541:Fluorescence Resonance Energy Transfer; D006863:Hydrogen-Ion Concentration; D056004:Molecular Dynamics Simulation; D016296:Mutagenesis; D011489:Protein Denaturation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D018035:Receptors, Odorant / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D013552:Swine
chemical_list: D000873:Anthracenes; D018035:Receptors, Odorant; C045648:odorant-binding protein; C049062:1-aminoanthracene