ANALYSIS OF PROTEINS AND PROTEOMES BY MASS SPECTROMETRY

A decade after the discovery of electrospray and matrix-assisted laser desorption ionization (MALDI), methods that finally allowed gentle ionization of large biomolecules, mass spectrometry has become a powerful tool in protein analysis and the key technology in the emerging field of proteomics. The...

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Bibliographic Details
Published in:Annual review of biochemistry 2001-01, Vol.70 (1), p.437-473
Main Authors: Mann, Matthias, Hendrickson, Ronald C, Pandey, Akhilesh
Format: Article
Language:English
Subjects:
Algorithms
Baits
Chromatography, Liquid - instrumentation
Chromatography, Liquid - methods
Databases, Protein
Electrophoresis, Gel, Two-Dimensional - methods
functional genomics
Genomics
Instrumentation
Ionization
Lasers
Mass spectrometry
Mass Spectrometry - instrumentation
Mass Spectrometry - methods
phosphorylation
posttranslational modifications
protein interaction
Protein Interaction Mapping - methods
Proteins
Proteins - analysis
Proteins - chemistry
Proteins - isolation & purification
proteomes
Proteomics
Scientific imaging
Sequence Analysis, Protein
Signal Transduction
Spectrometry, Mass, Electrospray Ionization - methods
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization - methods
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Summary:A decade after the discovery of electrospray and matrix-assisted laser desorption ionization (MALDI), methods that finally allowed gentle ionization of large biomolecules, mass spectrometry has become a powerful tool in protein analysis and the key technology in the emerging field of proteomics. The success of mass spectrometry is driven both by innovative instrumentation designs, especially those operating on the time-of-flight or ion-trapping principles, and by large-scale biochemical strategies, which use mass spectrometry to detect the isolated proteins. Any human protein can now be identified directly from genome databases on the basis of minimal data derived by mass spectrometry. As has already happened in genomics, increased automation of sample handling, analysis, and the interpretation of results will generate an avalanche of qualitative and quantitative proteomic data. Protein-protein interactions can be analyzed directly by precipitation of a tagged bait followed by mass spectrometric identification of its binding partners. By these and similar strategies, entire protein complexes, signaling pathways, and whole organelles are being characterized. Posttranslational modifications remain difficult to analyze but are starting to yield to generic strategies.
ISSN:0066-4154
1545-4509
DOI:10.1146/annurev.biochem.70.1.437