Efficiency of energy transfer in protonated diglycine and dialanine SID: Effects of collision angle, peptide ion size, and intramolecular potential

Jiangping Wang, Samy O. Meroueh, Yanfei Wang, William L. Hase

Research output: Contribution to journalArticle

39 Scopus citations


Classical trajectory simulations are performed to study energy transfer in collisions of protonated diglycine, (gly)2H+, and dialanine, (ala)2H+, ions with the diamond {111} surface, for a collision energy Ei in the range of 5-110eV and incident angles of 0 and 45° with respect to the surface normal. The distribution of energy transfer to vibrational/rotational degrees of freedom, ΔE int, and to the surface, ΔEsurf, and of energy remaining in peptide ion translation, Ef, are very similar for (gly)2H+ and (ala)2H+. The average percent energy transferred to ΔEsurf and Ef increases and decreases, respectively, with increase in Ei. Average energy transfer to ΔEint is less dependent on Ei, but does decrease with increase in Ei. The AMBER and AM1 models for the (gly)2H+ intramolecular potential give statistically identical energy transfer distributions in (gly)2H ++diamond {111} collisions. A comparison of the current study with previous trajectory simulations of glyH+, (gly)3H +, and (gly)5H+ collisions with diamond {111} shows that the energy transfer efficiencies to ΔEint, ΔEsurf, and Ef are similar for (gly) nH+, n=1-5. The energy transfer distributions for (gly)2H++diamond {111} collisions depend on the collision angle and do not scale in accord with the normal component of the collision energy Ei n for collisions with θi of 0 and 45°.

Original languageEnglish (US)
Pages (from-to)57-63
Number of pages7
JournalInternational Journal of Mass Spectrometry
Issue number1
StatePublished - Nov 1 2003



  • Energy transfer
  • Peptide ions
  • Surface-induced dissociation
  • Trajectory simulations

ASJC Scopus subject areas

  • Instrumentation
  • Condensed Matter Physics
  • Spectroscopy
  • Physical and Theoretical Chemistry

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