The atmospheric processing by ozone of peptide-containing mixed particles was investigated as proxies for biogenic and sea spray primary organic aerosol. Reactions were performed in a flow reactor and particle composition was monitored by photoelectron resonance capture ionization aerosol mass spectrometry. Mixed particles containing dipeptides in a saturated organic matrix of stearic and palmitic acids showed no reaction under ozonolysis at exposure levels of 2.5???10?4?atm s O3. However reactions of mixed particles of a dipeptide (Leu-Leu) in an unsaturated matrix (oleic acid) under the same conditions resulted in a rapid loss of the peptide ion signal, as well as the carrier matrix, and appearance of a number of ion signals corresponding to secondary products. High molecular weight imid...
A mixture of aminoacids was irradiated by a scattered proton beam, its energy varying from 4 to 6.6 MeV, by doses up to 5 x 10"1"1 proton/cm"2 for studying the potentiality of abiogenic synthesis of biologically important compounds in space. It was ascertained that increase in the radiation dose and reduction of proton energy involve increase in effectiveness both of destruction of the initial aminoacid (tryptophan, tyrosine, glycine) and synthesis of the relevant dipeptide. Essential influence of mineral substrate on abiogenic synthesis of natural nucleotides under the action of diverse energy sources was pointed out
The photoelectron resonance capture ionization (PERCI) of cysteine (Cys) and small gas-phase neutral peptides that contain the Cys residue (Cys-Gly, g-Glu-Cys, and glutathione (g-Glu-Cys-Gly)) is reported. At an ionization energy less than 1eV two types of dissociative electron attachment ionization were observed for Cys: hydrogen atom loss, resulting in formation of the ion [Cys-H]-, and dissociation of the CH2-SH bond, resulting in formation of the ion [SH]-. The presence of these ions suggests that both the p*(-CO2H) and *(C-S) orbitals can act as low energy electrophores on Cys. This ionization trend was observed for the dipeptides Cys-Gly and g-Glu-Cys as well as glutathione, with evidence that dissociation of the CH2-SH bond in these peptides can also result in ions of the form [M-SH...
We performed density functional calculations to examine the effects of solvation, hydrogen bonding, backbone conformation, and the side chain on 15N chemical shielding in proteins. We used N-methylacetamide (NMA) and N-formyl-alanyl-X (with X being one of the 19 naturally occurring amino acids excluding proline) as model systems. In addition, calculations were performed for selected fragments from protein GB3. The conducting polarizable continuum model was employed to include the effect of solvent in the density functional calculations. Our calculations for NMA show that the augmentation of the polarizable continuum model with the explicit water molecules in the first solvation shell has a significant influence on isotropic 15N chemical shift but not as much on the chemical shift anisotropy. The difference in the isotropic chemical shift between the standard ?-sheet and ?-helical conformations ranges from 0.8 to 6.2 ppm depending on the residue type, with the mean of 2.7 ppm. This is ...