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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 ?-barrel lipocalin scaffold.

SUBMITTER: Polverini E

PROVIDER: S-EPMC3127118 | biostudies-literature | 2011

REPOSITORIES: biostudies-literature

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Characterization of a deswapped triple mutant bovine odorant binding protein.

Polverini Eugenia E Lardi Paolo P Mazzini Alberto A Sorbi Robert T RT Virna Conti C Ramoni Roberto R Favilla Roberto R

International journal of molecular sciences 20110404 4

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 cha ...[more]

PMID: 21731442

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