PNNL

Abstract

The ability to quantify the changes in protein abundance between cells subjected to a variety of extracellular stimuli or the onset of a diseased state remains an extremely active area of proteome research. Although advances in sample preparation, chromatographic separation, mass spectrometry instrumentation and bioinformatics contribute to producing a viable method for comparative proteome-wide analyses, the foundation of quantitation is based in part upon improved methods for chemical and metabolic stable isotope labeling of proteins and peptides. The ability to quantify differences in protein expression and post-translational modifications has been demonstrated, but insights into the biochemical mechanisms that will contribute to the development of new biotechnologies have yet to be realized.