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Updated: Jun 28, 2026

Real-time In Vitro Monitoring of Odorant Receptor Activation by an Odorant in the Vapor Phase
Published on: April 23, 2019
Is asparagine deamidation in the porcine odorant-binding protein related to the odor molecules binding?
Gianfranco Mamone1, Sabato D'Auria
1Proteomic and Biomolecular Mass, Spectrometry Centre, ISA-CNR, Avellino, Italy.
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 beta-barrel structure and of the disulphide bridge. The internal cavity of the beta-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.
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