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lüll Analysis of posttranslational modifications of proteins by tandem mass spectrometry Larsen MR; Trelle MB; Thingholm TE; Jensen ONBiotechniques 2006[Jun]; 40 (6): 790-8Protein 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 protein. 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.|*Protein Processing, Post-Translational[MESH]|Mass Spectrometry[MESH]|Peptides/*chemistry[MESH] |