Jump to main content
Jump to site search


Mapping gas phase dipeptide motions in the far-infrared and terahertz domain

Author affiliations

Abstract

Vibrational signatures of Ac-Phe-AA-NH2 dipeptides are recorded and analysed in the far IR/THz spectral domain (100–800 cm−1, 3–24 THz), with the ‘AA’ amino acid chosen within the series ‘AA’ = Gly, Ala, Pro, Cys, Ser, Val. Phe stands for phenylalanine. IR-UV ion dip experiments are conducted on the free electron laser FELIX and combined with DFT-based molecular dynamics simulations for the calculation of the dynamical anharmonic vibrational spectra. The excellent agreements between the experimental and theoretical spectra of the Ac-Phe-AA-NH2 series allow us to make detailed and unambiguous mapping of the vibrational motions into three main domains: 700–800 cm−1 for C–H waggings, 400–700 cm−1 for N–H waggings, with a one-to-one signature per amide N–H backbone group, 0–400 cm−1 for delocalized and large amplitude collective motions over the dipeptide backbone, with backbone torsional motions arising <100 cm−1.

Graphical abstract: Mapping gas phase dipeptide motions in the far-infrared and terahertz domain

Back to tab navigation
Please wait while Download options loads

Supplementary files

Publication details

The article was received on 18 Jan 2017, accepted on 24 Apr 2017 and first published on 27 Apr 2017


Article type: Paper
DOI: 10.1039/C7CP00369B
Citation: Phys. Chem. Chem. Phys., 2017, Advance Article
  •   Request permissions

    Mapping gas phase dipeptide motions in the far-infrared and terahertz domain

    J. Mahé, D. J. Bakker, S. Jaeqx, A. M. Rijs and M. Gaigeot, Phys. Chem. Chem. Phys., 2017, Advance Article , DOI: 10.1039/C7CP00369B

Search articles by author