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

@article{Stepanenko2016StructureAS,
  title={Structure and stability of recombinant bovine odorant-binding protein: II. Unfolding of the monomeric forms.},
  author={Olga V. Stepanenko and Denis O. Roginskii and Olesya V Stepanenko and Irina M. Kuznetsova and Vladimir N. Uversky and Konstantin K Turoverov},
  journal={PeerJ},
  year={2016},
  volume={4},
  pages={e1574}
}
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 monomeric variants, the bOBP-Gly121+ mutant containing an additional glycine residue after the residue 121 of the bOBP, and the GCC-bOBP mutant obtained from the bOBP-Gly121+ form by introduction of the… CONTINUE READING
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