Journal of Atomic, Molecular, and Optical Physics
Volume 2011 (2011), Article ID 356589, 6 pages
Grazing Molecule Excitation as a Tool to Analyse the Amino Acid Sequence in Oligopeptides
1Faculty of Chemistry, Philipps University of Marburg, 35032 Marburg, Germany
2Skobeltsyn Institute of Nuclear Physics, Lomonossov Moscow State University, Moscow 119991, Russia
Received 10 June 2011; Accepted 14 August 2011
Academic Editor: Colm T. Whelan
Copyright © 2011 H. Jungclas et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
A novel mass spectrometric method to analyse the sequence of amino acid residues in oligopeptides is proposed. Amino acid residues in peptide molecules contain chain-like structures of identical CH dipoles (IR antennas), which acquire IR energy quanta by interaction with periodic Coulomb fields and accumulate vibration excitation energy. This can subsequently lead to the dissociation of specific trap bonds inside the peptide molecule. Such excitation and dissociation processes are assumed to occur when peptide ions graze at atomic distance along a set of screened charges on a surface. These processes of grazing molecule excitation (GME) and dissociation (GMD) were applied to analyse sequences of oligopeptides by using TOF mass spectrometry. At specific grazing velocities the experimental fragment ion spectra of oligopeptides must contain a peak of high abundance corresponding to the N-terminal amino acid. This specific property of GMD offers the possibility to determine the amino acid sequence of oligopeptides.