Title
Structure and Stability of Recombinant Bovine Odorant-Binding Protein: Iii. Peculiarities of the Wild Type Bobp Unfolding in Crowded Milieu
Document Type
Article
Publication Date
2015
Keywords
odorant-binding protein, macromoleclar crowding, disulfide bond, ligand binding, conformational stability, domain swapping, unfolding-refolding reaction
Digital Object Identifier (DOI)
https://doi.org/10.7287/peerj.preprints.1454v1
Abstract
Contrarily to the majority of the members of the lipocalin family, which are stable monomers with the specific OBP fold (a β-barrel consisting of a 8-stranded anti-parallel β-sheet followed by a short α-helical segment, a ninth β-strand, and a disordered C-terminal tail) and a conserved disulfide bond, bovine odorant-binding protein (bOBP) does not have such a disulfide bond and forms a domain-swapped dimer that involves crossing the α-helical region from each monomer over the β-barrel of the other monomer. Furthermore, although natural bOBP isolated from bovine tissues exists as a stable domain-swapped dimer, recombinant bOBP has decreased dimerization potential and therefore exists as a mixture of monomeric and dimeric variants. In this article, we investigated the effect model crowding agents of similar chemical nature but different molecular mass on conformational stability of the recombinant bOBP. These experiments were conducted in order shed light on the potential influence of model crowded environment on the unfolding-refolding equilibrium. To this end, we looked at the influence of PEG-600, PEG-4000, and PEG-12000 in concentrations of 80, 150, and 300 mg/mL on the equilibrium unfolding and refolding transitions induced in the recombinant bOBP by guanidine hydrochloride.
Rights Information
This work is licensed under a Creative Commons Attribution 4.0 License.
Was this content written or created while at USF?
Yes
Citation / Publisher Attribution
Peerj, v. 3, art. e1454v1
Scholar Commons Citation
Stepanenko, Olga V.; Roginskii, Denis O.; Stepanenko, Olesya V.; Kuznetsova, Irina M.; Uversky, Vladimir N.; and Turoverov, Konstantin K., "Structure and Stability of Recombinant Bovine Odorant-Binding Protein: Iii. Peculiarities of the Wild Type Bobp Unfolding in Crowded Milieu" (2015). Molecular Medicine Faculty Publications. 39.
https://digitalcommons.usf.edu/mme_facpub/39