Ontology highlight
ABSTRACT:
SUBMITTER: Stepanenko OV
PROVIDER: S-EPMC4841237 | biostudies-literature | 2016
REPOSITORIES: biostudies-literature
Stepanenko Olga V OV Roginskii Denis O DO Stepanenko Olesya V OV Kuznetsova Irina M IM Uversky Vladimir N VN Turoverov Konstantin K KK
PeerJ 20160418
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 T ...[more]