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

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...

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Auteurs principaux:	Olga V. Stepanenko, Denis O. Roginskii, Olesya V. Stepanenko, Irina M. Kuznetsova, Vladimir N. Uversky, Konstantin K. Turoverov
Format:	Artigo
Langue:	Inglês
Publié:	PeerJ Inc. 2016-04-01
Collection:	PeerJ
Sujets:	Odorant-binding protein Macromolecular crowding Disulfide bond Ligand binding Conformational stability Domain swapping
Accès en ligne:	https://peerj.com/articles/1642.pdf
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