The processes of negative ions formation of dipeptides glycyl-glycine, glycyl-alanine and alanyl-alanine in the conditions of resonant electron capture have been studied with a help of negative ions mass spectrometry. Using a thermochemical approach, the main channels of fragment negative ions formation were found and the structure of the ions were established. The isobaric ions have been identified by the experiments with high mass resolution. The cross sections of fragment ions formation were measured. The metastable fragmentation of [M-H](-) and [M-COOH](-) ions in the energy range 4.5-7.5 eV have been found.

We present experimental and theoretical study of electron ionization and dissociative ionization to the gas phase amino acids valine, leucine, and isoleucine. A crossed electron/molecular beams technique equipped with quadrupole mass analyzer has been applied to measure mass spectra and ion efficiency curves for formation of particular ions. From experimental data the ionization energies of the molecules and the appearance energies of the fragment ions were determined. Ab initio calculations (Density Functional Theory and G3MP2 methods) were performed in order to calculate the fragmentation paths and interpret the experimental data. The experimental ionization energies of parent molecules [P](+) 8.91 ± 0.05, 8.85 ± 0.05, and 8.79 ± 0.05 eV and G3MP2 ionization energies (adiabatic) of 8.89, 8.88, and 8.81 eV were determined for valine, leucine, and isoleucine, respectively, as well as the experimental and theoretical threshold energies for dissociative ionization channels. The comparison of experimental data with calculations resulted in identification of the ions as well as the neutral fragments formed in the dissociative reactions. Around 15 mass/charge ratio fragments were identified from the mass spectra by comparison of experimental appearance energies with calculated reaction enthalpies for particular dissociative reactions.

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