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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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| Publicado no: | PeerJ |
|---|---|
| Main Authors: | , , , , , |
| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
PeerJ Inc.
2016
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| Assuntos: | |
| Acesso em linha: | https://ncbi.nlm.nih.gov/pmc/articles/PMC4841250/ https://ncbi.nlm.nih.gov/pubmed/27114880 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.7717/peerj.1933 |
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