Tandem Mass Spectrometric Characterization of Modified Peptides and Proteins

  • Simon J. Gaskell
  • Mark S. Bolgar
  • Kathleen A. Cox


Mass spectrometry (MS) is now widely accepted as an analytical technique of complementary value to Edman-based approaches to peptide and protein structure determination. The value of MS derives from the accommodation of mixtures and the possibilities for characterization of modified amino acid residues. Tandem MS in particular is important in addressing both of these issues. The essential features of tandem MS are the promotion of ion fragmentation (generally following collision with a target gas) and the establishment of connectivity between precursor and product ions. Such analyses can yield structural information for individual components of mixtures. A variety of instrumental techniques have been used for tandem MS, differing in the choice of ion analyzers and the precise experimental conditions under which precursor ion activation and decomposition take place. Thus, for example, tandem MS of peptides using four-sector mass spectrometers generally involves high energy collisional activation of precursor ions (usually [M+H]+) to promote fragmentations indicative of sequence and permitting the differentiation of isomeric/isobaric amino acid residues [1].


Collisional Activation Cysteic Acid Tandem Mass Spectrometry Analysis Precise Experimental Condition Modify Amino Acid Residue 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


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Copyright information

© Springer Science+Business Media New York 1995

Authors and Affiliations

  • Simon J. Gaskell
    • 1
  • Mark S. Bolgar
    • 1
  • Kathleen A. Cox
    • 1
  1. 1.Michael Barber Centre for Mass Spectrometry Department of ChemistryUniversity of Manchester Institute of Science and Technology (UMIST)ManchesterUK

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