Mass Spectrometry of Peptides and Proteins

Abstract Originally published in: Proteomics in Drug Research. Edited by Michael Hamacher, Katrin Marcus, Kai Stühler, André van Hall, Bettina Warscheid and Helmut E. Meyer. Copyright © 2006 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐31226‐9 Rapid advances in biological mass spectrometry have promoted proteomics to being a key technology in molecular cell biology and biomedical research. Current mass spectrometry‐based proteomics provides the capability for the identification of cellular and subcellular proteomes, the study of changes in protein concentrations via stable isotope labeling methods and the mapping of functional protein modules isolated by means of affinity purification. The large potential of proteomics techniques to identify and accurately quantify proteins from complex biological samples has been well recognized in the larger scientific community and it will in all probability have a great impact on future drug research. The sections in this article are Introduction Ionization Principles Matrix‐Assisted Laser Desorption/Ionization ( MALDI ) Electrospray Ionization Mass Spectrometric Instrumentation Protein Identification Strategies Quantitative Mass Spectrometry for Comparative and Functional Proteomics Metabolic Labeling Approaches 15 N Labeling Stable Isotope Labeling by Amino Acids in Cell Culture ( SILAC ) Chemical Labeling Approaches Chemical Isotope Labeling at the Protein Level Stable Isotope Labeling at the Peptide Level Quantitative MS for Deciphering Protein‐Protein Interactions Conclusions Acknowledgements