ABSTRACT
Soon after the introduction of electrospray ionization (ESI) and matrix-assisted laser desorption ionization (MALDI) for mass spectrometry (MS) in 1988, these techniques were intensively applied to the characterization of peptides and proteins. After initial studies, discussed in Ch. 16, significant new developments started in the mid-1990s. Step-by-step developments of technologies and procedures of protein characterization brought us to where we stand today. Nowadays, high-throughput liquid chromatography–mass spectrometry (LC–MS) analysis of tryptic digests and multidimensional LC–MS of digests of the complete proteome of a bacteria or of human plasma are routinely performed in many laboratories. Interpretation of product-ion MS–MS spectra of individual tryptic peptides has been replaced by automated database searching of multidimensional data sets. Currently, ESI-MS and MALDI-MS play a prominent role in the field of proteomics. The advent and development of these enabling technologies are highlighted in this chapter. This chapter is a technology overview rather than a comprehensive review of current applications of LC–MS of peptides.
