Analysis of posttranslational modifications of proteins by tandem mass spectrometry

Martin R. Larsen, Morten B. Trelle, Tine E. Thingholm, Ole N. Jensen
2006 BioTechniques  
Protein activity and turnover is tightly and dynamically regulated in living cells. Whereas the three-dimensional protein structure is predominantly determined by the amino acid sequence, posttranslational modification (PTM) of proteins modulates their molecular function and the spatial-temporal distribution in cells and tissues. Most PTMs can be detected by protein and peptide analysis by mass spectrometry (MS), either as a mass increment or a mass deficit relative to the nascent unmodified
more » ... tein. Tandem mass spectrometry (MS/MS) provides a series of analytical features that are highly useful for the characterization of modified proteins via amino acid sequencing and specific detection of posttranslationally modified amino acid residues. Large-scale, quantitative analysis of proteins by MS/MS is beginning to reveal novel patterns and functions of PTMs in cellular signaling networks and biomolecular structures.
doi:10.2144/000112201 pmid:16774123 fatcat:uczz5e2kprhbjmvjmi5pdh5i2q