Mass Spectrometry of Peptides and Proteins up to Proteomics

Abstract The development of mass spectrometric methodologies for determining the amino acid sequences of peptides and the primary structure of proteins began in the late 1950s with the conversion of small peptides to analogous polyamino alcohols that were sufficiently volatile to be separated by gas chromatography and ionized by electron impact. Sequencing was greatly simplified by the ability to ionize intact peptides and even entire proteins directly afforded by the invention of FAB, MALDI, and ESI in the 1980s. The advent of DNA sequencing provided further synergistic avenues to the efficient determination of the primary structure of even very large proteins.