Mass Spectrometry in Protein Structural Analysis

Abstract

Mass spectrometric protein analysis was pioneered in the 1960s and early 1970s by K. Biemann and co-workers at MIT, E. Lederer’s group at the Institute for Natural Product Chemistry in Gif sur Yvette, France, in collaboration with M. Barber at AEI, and at the Shemyakin Institute for Natural Product Chemistry in Moscow. The mass spectrometric techniques at that time required volatile samples that, because of the zwitter ionic nature of peptides, required derivatization. Ionization was performed by electron impact, resulting in high excitation of the formed ions and subsequent extensive fragmentation. As a result, only rather small peptides were amenable to mass spectrometric analysis. The development of new ionization methods in the 1970s such as chemical ionization and field desorption, although promising, did not improve the perspectives for mass spectrometric protein analysis. In spite of these limitations, mass spectrometric research, carried out in a rather limited number of groups, made significant contributions to protein research, especially in characterization of posttranslationally modified amino acid residues and sequencing of N-terminally blocked peptides (reviewed, for exam-ple, in Arpino and McLafferty, 1976).