Analysis of posttranslational modifications of proteins by tandem mass spectrometry

Biotechniques. 2006 Jun;40(6):790-8. doi: 10.2144/000112201.


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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Mass Spectrometry
  • Peptides / chemistry*
  • Protein Processing, Post-Translational*


  • Peptides