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

Characterization of a Deswapped Triple Mutant Bovine Odorant Binding Protein

Department of Physics and CNISM, University of Parma, V.le Usberti 7A, Parma, Italy
Department of Animal Production, Veterinary Biotechnologies, Food Quality and Safety, University of Parma, V. del Taglio 8, Parma, Italy
Department of Biochemistry and Molecular Biology, University of Parma, V.le Usberti 23A, Parma, Italy
Author to whom correspondence should be addressed.
Received: 1 March 2011 / Revised: 16 March 2011 / Accepted: 29 March 2011 / Published: 4 April 2011
(This article belongs to the Special Issue Protein Folding 2011)
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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 odorant binding proteins; unfolding/refolding; molecular dynamics

This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

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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.

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