Structure and stability of recombinant bovine odorant-binding protein: II. Unfolding of the monomeric forms

Structure and stability of recombinant bovine odorant-binding protein: II. Unfolding of the monomeric forms

In a family of monomeric odorant-binding proteins (OBPs), bovine OBP (bOBP), that lacks conserved disulfide bond found in other OBPs, occupies unique niche because of its ability to form domain-swapped dimers. In this study, we analyzed conformational stabilities of the recombinant bOBP and its mono...

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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
Ligand binding
Disulfide bond
Domain swapping
Unfolding-refolding reaction
Conformational stability
Online Access:https://peerj.com/articles/1574.pdf

Internet

https://peerj.com/articles/1574.pdf

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