Is Asparagine Deamidation in the Porcine Odorant-Binding Protein Related to the Odor Molecules Binding?

Title: Is Asparagine Deamidation in the Porcine Odorant-Binding Protein Related to the Odor Molecules Binding?

Volume: 15 Issue: 9

Author(s): Gianfranco Mamone and Sabato D'Auria

Affiliation:

Keywords: Deamidation, mass spectrometry, odorant-binding protein, odorant molecules

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

Cite this article as:

Mamone Gianfranco and D'Auria Sabato, Is Asparagine Deamidation in the Porcine Odorant-Binding Protein Related to the Odor Molecules Binding?, Protein & Peptide Letters 2008; 15 (9) . https://dx.doi.org/10.2174/092986608785849344