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...
| Main Authors: | , , , , , |
|---|---|
| Format: | Online |
| Language: | English |
| Published: |
PeerJ Inc.
2016
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| Online Access: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4841237/ |