Mass spectrometry--a key technology in proteome research.
The rapid developments in the field of mass spectrometry have transformed it into a key technology in proteome research. Increased sensitivity in mass spectrometry, as a result of more efficient ionisation techniques and better detectors, has allowed the stepwise reduction of protein quantity for analysis. Protein spots of 2D-PAGE separated samples are now quantitatively sufficient for an unequivocal identification of a protein by mass spectrometry. In addition to protein identification a closer look at posttranslational modifications is now also possible. It is speculated that modifications like phosphorylation or glycosylation exist on every second protein and that they are important for the protein function. This review highlights the different mass spectrometric methods and gives a brief overview of strategies and methods used to identify modifications.
Sickmann
Albert
A
Rudolf-Virchow-Zentrum, DFG Forschungszentrum für Experimentelle Biomedizin, Versbacher Strasse 9, Raum 411, 97078 Würzburg, Germany. Albert.Sickmann@virchow.uni-wuerzburg.de
Mreyen
Marcus
M
Meyer
Helmut E
HE
D000595:Amino Acid Sequence; D006019:Glycolysis; D013058:Mass Spectrometry / Q000295:instrumentation / Q000379:methods* / Q000639:trends; D008969:Molecular Sequence Data; D010766:Phosphorylation; D011499:Protein Processing, Post-Translational; D020543:Proteome / Q000032:analysis* / Q000737:chemistry* / Q000378:metabolism; D020539:Sequence Analysis, Protein / Q000379:methods*; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / Q000295:instrumentation / Q000379:methods
D020543:Proteome