Int. J. Mol. Sci. 2011, 12(4), 2294-2314; doi:10.3390/ijms12042294
Article

Characterization of a Deswapped Triple Mutant Bovine Odorant Binding Protein

1email, 1email, 1email, 1email, 2email, 2email and 3,* email
Received: 1 March 2011; in revised form: 16 March 2011 / Accepted: 29 March 2011 / Published: 4 April 2011
(This article belongs to the Special Issue Protein Folding 2011)
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
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.
Keywords: odorant binding proteins; unfolding/refolding; molecular dynamics
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MDPI and ACS Style

Polverini, E.; Lardi, P.; Mazzini, A.; Sorbi, R.T.; Virna, C.; Ramoni, R.; Favilla, R. Characterization of a Deswapped Triple Mutant Bovine Odorant Binding Protein. Int. J. Mol. Sci. 2011, 12, 2294-2314.

AMA Style

Polverini E, Lardi P, Mazzini A, Sorbi RT, Virna C, Ramoni R, Favilla R. Characterization of a Deswapped Triple Mutant Bovine Odorant Binding Protein. International Journal of Molecular Sciences. 2011; 12(4):2294-2314.

Chicago/Turabian Style

Polverini, Eugenia; Lardi, Paolo; Mazzini, Alberto; Sorbi, Robert T.; Virna, Conti; Ramoni, Roberto; Favilla, Roberto. 2011. "Characterization of a Deswapped Triple Mutant Bovine Odorant Binding Protein." Int. J. Mol. Sci. 12, no. 4: 2294-2314.

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