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

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...

Full description

Bibliographic Details
Main Authors: Olga V. Stepanenko, Denis O. Roginskii, Olesya V. Stepanenko, Irina M. Kuznetsova, Vladimir N. Uversky, Konstantin K. Turoverov
Format: Article
Language:English
Published: PeerJ Inc. 2016-04-01
Series:PeerJ
Subjects:
Odorant-binding protein
Macromolecular crowding
Disulfide bond
Ligand binding
Conformational stability
Domain swapping
Online Access:https://peerj.com/articles/1642.pdf

Internet

https://peerj.com/articles/1642.pdf

Similar Items