Proteome analysis by mass spectrometry.

TitleProteome analysis by mass spectrometry.
Publication TypeJournal Article
Year of Publication2003
AuthorsFerguson, PL, Smith, RD
JournalAnnual Review of Biophysics and Biomolecular Structure
Start Page399
Pagination399 - 424
Date Published01/2003

The coupling of high-performance mass spectrometry instrumentation with highly efficient chromatographic and electrophoretic separations has enabled rapid qualitative and quantitative analysis of thousands of proteins from minute samples of biological materials. Here, we review recent progress in the development and application of mass spectrometry-based techniques for the qualitative and quantitative analysis of global proteome samples derived from whole cells, tissues, or organisms. Techniques such as multidimensional peptide and protein separations coupled with mass spectrometry, accurate mass measurement of peptides from global proteome digests, and mass spectrometric characterization of intact proteins hold great promise for characterization of highly complex protein mixtures. Advances in chemical tagging and isotope labeling techniques have enabled quantitative analysis of proteomes, and highly specific isolation strategies have been developed aimed at selective analysis of posttranslationally modified proteins.

Short TitleAnnual Review of Biophysics and Biomolecular Structure