Skip to content
2000
Volume 15, Issue 9
  • ISSN: 0929-8665
  • E-ISSN: 1875-5305

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 β-barrel structure and of the disulphide bridge. The internal cavity of the β-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

Loading

Article metrics loading...

/content/journals/ppl/10.2174/092986608785849344
2008-09-01
2025-05-22
Loading full text...

Full text loading...

/content/journals/ppl/10.2174/092986608785849344
Loading

  • Article Type:
    Research Article
Keyword(s): Deamidation; mass spectrometry; odorant molecules; odorant-binding protein
This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error
Please enter a valid_number test