Analysis of posttranslational modifications of proteins by tandem mass spectrometry.
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 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.
Larsen
Martin R
MR
University of Southern Denmark, Odense M, Denmark.
Trelle
Morten B
MB
Thingholm
Tine E
TE
Jensen
Ole N
ON
D013058:Mass Spectrometry; D010455:Peptides / Q000737:chemistry*; D011499:Protein Processing, Post-Translational
D010455:Peptides