|Publication Type||Journal Article|
|Year of Publication||2005|
|Authors||Ong, S-E, Mann, M|
|Journal||Nat Chem Biol|
|Date Published||2005 Oct|
|Keywords||Base Sequence, Isotope Labeling, Mass Spectrometry, Molecular Sequence Data, Molecular Structure, Proteomics, Quantitative Structure-Activity Relationship|
The field of proteomics is built on technologies to analyze large numbers of proteins--ideally the entire proteome--in the same experiment. Mass spectrometry (MS) has been successfully used to characterize proteins in complex mixtures, but results so far have largely been qualitative. Two recently developed methodologies offer the opportunity to obtain quantitative proteomic information. Comparing the signals from the same peptide under different conditions yields a rough estimate of relative protein abundance between two proteomes. Alternatively, and more accurately, peptides are labeled with stable isotopes, introducing a predictable mass difference between peptides from two experimental conditions. Stable isotope labels can be incorporated 'post-harvest', by chemical approaches or in live cells through metabolic incorporation. This isotopic handle facilitates direct quantification from the mass spectra. Using these quantitative approaches, precise functional information as well as temporal changes in the proteome can be captured by MS.
|Alternate Journal||Nat. Chem. Biol.|