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Structure and stability of recombinant bovine odorant-binding protein: I. Design and analysis of monomeric mutants

Bovine odorant-binding protein (bOBP) differs from other lipocalins by lacking the conserved disulfide bond and for being able to form the domain-swapped dimers. To identify structural features responsible for the formation of the bOBP unique dimeric structure and to understand the role of the domai...

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Principais autores: Olga V. Stepanenko, Denis O. Roginskii, Olesya V. Stepanenko, Irina M. Kuznetsova, Vladimir N. Uversky, Konstantin K. Turoverov
Format: Artigo
Sprog:Inglês
Udgivet: PeerJ Inc. 2016-04-01
Serier:PeerJ
Fag:
Odorant-binding protein
Fluorescence
Protein
Domain swapping
Chemical denaturation
Circular dichroism
Online adgang:https://peerj.com/articles/1933.pdf
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