High resolution mass analysis of N- and C-terminal negative ions resulting from resonance electron capture by aliphatic amino acids
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Updated: Jun 12, 2026

Analyzing Large Protein Complexes by Structural Mass Spectrometry
Published on: June 19, 2010
Pavel V Shchukin1, Mars V Muftakhov, Jeff Morré
1Institute of Physics of Molecules and Crystals, Ufa Research Center, Russian Academy of Science, Ufa 450075, Russia.
Abstract:
High mass resolving power was applied to study resonance electron capture by glycine, alanine, and valine, and accurate mass measurements helped to distinguish between some negative ions having the same nominal masses. It was established that the C- and N-terminal negative ions of the same nominal masses were formed at different electron energies from different resonance states. The typical fragmentation pathways in deprotonated amino acids via loss of water initiated by collisional activation were not observed upon resonant electron capture by aliphatic amino acids. Instead, [M-18](-) negative ions in the vicinity of 5 eV were found to be associated with simultaneous loss of either ammonia and a hydrogen atom or an amino group and a hydrogen molecule.
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