http://www.cnr.it/ontology/cnr/individuo/prodotto/ID168212
Is asparagine deamidation in the porcine odorant-binding protein related to the odour molecules binding? (Articolo in rivista)
- Type
- Label
- Is asparagine deamidation in the porcine odorant-binding protein related to the odour molecules binding? (Articolo in rivista) (literal)
- Anno
- 2008-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.2174/092986608785849344 (literal)
- Alternative label
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Mamone G., D'Auria S. (literal)
- Pagina inizio
- Pagina fine
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
- Rivista
- Note
- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- Istituto scienze dell'Alimentazione, CNR Avellino
Istituto di Biochimica delle Proteine (literal)
- Titolo
- Is asparagine deamidation in the porcine odorant-binding protein related to the odour molecules binding? (literal)
- Abstract
- Odorant-binding proteins are biomolecules belonging to the lipocalin family. Among all the odorant-binding proteins, the porcine odorant-binding protein has been well characterized. This protein is a monomer that is characterized by the presence of the ²-barrel structure and of the disulphide bridge. The internal cavity of the ²-barrel is the binding site. In this study we have investigated the structural properties of the porcine odorant-binding protein by mass spectrometry experiments. Our data allow us to hypothesize that specific deamidation mechanisms of specific amino acid residues can be responsible for the binding properties of this class of proteins (literal)
- Prodotto di
- Autore CNR
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