Conformational Stability and Binding Properties of Porcine Odorant Binding Protein

Biochemistry ◽  
1999 ◽  
Vol 38 (45) ◽  
pp. 15043-15051 ◽  
Author(s):  
Tatiana V. Burova ◽  
Yvan Choiset ◽  
Christophe K. Jankowski ◽  
Thomas Haertlé
Keyword(s):  
Binding Protein ◽  
Conformational Stability ◽  
Odorant Binding Protein ◽  
Binding Properties ◽  
Odorant Binding ◽  
Porcine Odorant Binding Protein

Stability and Dynamics of the Porcine Odorant-Binding Protein†

Biochemistry ◽  
2007 ◽  
Vol 46 (39) ◽  
pp. 11120-11127 ◽  
Author(s):  
Maria Staiano ◽  
Sabato D'Auria ◽  
Antonio Varriale ◽  
Mose' Rossi ◽  
Anna Marabotti ◽  
...  
Keyword(s):  
Binding Protein ◽  
Odorant Binding Protein ◽  
Odorant Binding ◽  
Porcine Odorant Binding Protein

The Structure of the Monomeric Porcine Odorant Binding Protein Sheds Light on the Domain Swapping Mechanism‡

Biochemistry ◽  
1998 ◽  
Vol 37 (22) ◽  
pp. 7913-7918 ◽  
Author(s):  
Silvia Spinelli ◽  
Roberto Ramoni ◽  
Stefano Grolli ◽  
Jacques Bonicel ◽  
Christian Cambillau ◽  
...  
Keyword(s):  
Binding Protein ◽  
Odorant Binding Protein ◽  
Domain Swapping ◽  
Odorant Binding ◽  
Porcine Odorant Binding Protein

scholarly journals The porcine odorant-binding protein as molecular probe for benzene detection

PLoS ONE ◽  
2018 ◽  
Vol 13 (9) ◽  
pp. e0202630 ◽  
Author(s):  
Alessandro Capo ◽  
Angela Pennacchio ◽  
Antonio Varriale ◽  
Sabato D'Auria ◽  
Maria Staiano
Keyword(s):  
Binding Protein ◽  
Odorant Binding Protein ◽  
Molecular Probe ◽  
Odorant Binding ◽  
Porcine Odorant Binding Protein

Evidence of an Odorant-Binding Protein in the Human Olfactory Mucus:  Location, Structural Characterization, and Odorant-Binding Properties†

Biochemistry ◽  
2002 ◽  
Vol 41 (23) ◽  
pp. 7241-7252 ◽  
Author(s):  
Loïc Briand ◽  
Corinne Eloit ◽  
Claude Nespoulous ◽  
Valérie Bézirard ◽  
Jean-Claude Huet ◽  
...  
Keyword(s):  
Structural Characterization ◽  
Binding Protein ◽  
Odorant Binding Protein ◽  
Binding Properties ◽  
Odorant Binding

Hydrophobic interactions and ionic networks play an important role in thermal stability and denaturation mechanism of the porcine odorant-binding protein

2008 ◽  
Vol 71 (1) ◽  
pp. 35-44 ◽  
Author(s):  
Olesya V. Stepanenko ◽  
Anna Marabotti ◽  
Irina M. Kuznetsova ◽  
Konstantin K. Turoverov ◽  
Carlo Fini ◽  
...  
Keyword(s):  
Thermal Stability ◽  
Hydrophobic Interactions ◽  
Binding Protein ◽  
Odorant Binding Protein ◽  
Odorant Binding ◽  
Porcine Odorant Binding Protein

scholarly journals Structure and stability of recombinant bovine odorant-binding protein: III. Peculiarities of the wild type bOBP unfolding in crowded milieu

PeerJ ◽  
2016 ◽  
Vol 4 ◽  
pp. e1642 ◽  
Author(s):  
Olga V. Stepanenko ◽  
Denis O. Roginskii ◽  
Olesya V. Stepanenko ◽  
Irina M. Kuznetsova ◽  
Vladimir N. Uversky ◽  
...  
Keyword(s):  
Disulfide Bond ◽  
Binding Protein ◽  
Guanidine Hydrochloride ◽  
Conformational Stability ◽  
Odorant Binding Protein ◽  
Stable Domain ◽  
Peg 4000 ◽  
Similar Chemical ◽  
High Concentrations ◽  
Odorant Binding

Contrary 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 to 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. We are showing here that the effect of crowding agents on the structure and conformational stability of the recombinant bOBP depends on the size of the crowder, with the smaller crowding agents being more effective in the stabilization of the bOBP native dimeric state against the guanidine hydrochloride denaturing action. This effect of the crowding agents is concentration dependent, with the high concentrations of the agents being more effective.

Sign in / Sign up

Export Citation Format

Share Document