Chemistry meets proteomics: the use of chemical tagging reactions for MS-based proteomics.
As proteomics matures from a purely descriptive to a function-oriented discipline of the life sciences, there is strong demand for novel methodologies that increase the depth of information that can be obtained from proteomic studies. MS has long played a central role for protein identification and characterization, often in combination with dedicated chemical modification reactions. Today, chemistry is helping to advance the field of proteomics in numerous ways. In this review, we focus on those methodologies that have a significant impact for the large-scale study of proteins and peptides. This includes approaches that allow the introduction of affinity tags for the enrichment of subclasses of peptides or proteins and strategies for in vitro stable isotope labeling for quantification purposes, among others. Particular attention is given to the study of PTMs where recent advancements have been promising, but many interesting targets are not yet being addressed.
Leitner
Alexander
A
Department of Analytical Chemistry and Food Chemistry, University of Vienna, Vienna, Austria. alexander.leitner@univie.ac.at
Lindner
Wolfgang
W
D000818:Animals; D001671:Biochemistry / Q000295:instrumentation / Q000379:methods*; D002244:Carbon / Q000737:chemistry; D002462:Cell Membrane / Q000737:chemistry*; D002621:Chemistry / Q000379:methods; D002845:Chromatography; D006031:Glycosylation; D006801:Humans; D007554:Isotopes; D013058:Mass Spectrometry / Q000295:instrumentation / Q000379:methods*; D008745:Methylation; D008956:Models, Chemical; D010455:Peptides / Q000737:chemistry; D010766:Phosphorylation; D040901:Proteomics / Q000295:instrumentation / Q000379:methods*
D007554:Isotopes; D010455:Peptides; D002244:Carbon