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 beta-barrel lipocalin scaffold.
Characterization of a Deswapped Triple Mutant Bovine Odorant Binding Protein / Polverini, Eugenia; P., Lardi; Mazzini, Alberto; Sorbi, Robert Tibor; Conti, Virna; Ramoni, Roberto; Favilla, Roberto. - In: INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES. - ISSN 1661-6596. - 12:(2011), pp. 2294-2314. [10.3390/ijms12042294]
Characterization of a Deswapped Triple Mutant Bovine Odorant Binding Protein
POLVERINI, Eugenia;MAZZINI, Alberto;SORBI, Robert Tibor;CONTI, Virna;RAMONI, Roberto;FAVILLA, Roberto
2011-01-01
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 beta-barrel lipocalin scaffold.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.