Journal of the American Chemical Society, Vol.124, No.7, 1524-1531, 2002
Dynamics of energy transfer in peptide-surface collisions
Classical trajectory simulations are performed to study energy transfer in collisions of protonated triglycine (Gly)(3) and pentaglycine (Gly)(5) ions with n-hexyl thiolate self-assembled monolayer (SAM) and diamond {111} surfaces, for a collision energy E-i in the range of 10-110 eV and a collision angle of 45degrees. Energy transfer to the peptide ions' internal degrees of freedom is more efficient for collision with the diamond surface; i.e., 20% transfer to peptide vibration/rotation at E-i = 30 eV. For collision with diamond, the majority of E-i remains in peptide translation, while the majority of the energy transfer is to surface vibrations for collision with the softer SAM surface. The energy-transfer efficiencies are very similar for (Gly)(3) and (Gly)(5). Constraining various modes of (Gly)3 shows that the peptide torsional modes absorb similar to80% of the energy transfer to the peptide's internal modes. The energy-transfer efficiencies depend on E, These simulations are compared with recent experiments of peptide SID and simulations of energy transfer in Cr(CO)(6)(+) collisions with the SAM and diamond surfaces.