Identification and quantification of the enantiomeric excess of O-phosphoserine (OPSer) residues from post-translational modified proteins is now possible by the application of a very reproducible and sensitive mass spectrometric method. This technique is based on the different mass-spectral fragmentation patterns of the diastereomeric cluster ions generated in water/methanol solutions of the analyte (OPSerD/L) with a suitable chiral compound (OPThrL) by collision-induced dissociation (CID; see mass spectra).

Chiral recognition of O-phosphoserine by mass spectrometry

Paladini A;
2001

Abstract

Identification and quantification of the enantiomeric excess of O-phosphoserine (OPSer) residues from post-translational modified proteins is now possible by the application of a very reproducible and sensitive mass spectrometric method. This technique is based on the different mass-spectral fragmentation patterns of the diastereomeric cluster ions generated in water/methanol solutions of the analyte (OPSerD/L) with a suitable chiral compound (OPThrL) by collision-induced dissociation (CID; see mass spectra).
2001
Istituto di Struttura della Materia - ISM - Sede Roma Tor Vergata
Chirality
Enantioselectivity
Mass spectrometry
Proteomics
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/20.500.14243/201915
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