Characterization of a Deswapped Triple Mutant Bovine Odorant Binding Protein

International Journal of Molecular Sciences

Eugenia Polverini²  Paolo Lardi²  Alberto Mazzini²  Robert T. Sorbi²  Conti Virna¹  Roberto Ramoni¹ 

[1] Department of Animal Production, Veterinary Biotechnologies, Food Quality and Safety, University of Parma, V. del Taglio 8, Parma, Italy; E-Mails:;Department of Physics and CNISM, University of Parma, V.le Usberti 7A, Parma, Italy; E-Mails:

关键词: odorant binding proteins;    unfolding/refolding;    molecular dynamics;   

DOI  :  10.3390/ijms12042294

来源: mdpi

【 摘 要 】

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.

【 授权许可】

CC BY   
© 2011 by the authors; licensee MDPI, Basel, Switzerland.