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Updated: Mar 2, 2026

Infrared Degenerate Four-wave Mixing with Upconversion Detection for Quantitative Gas Sensing
Published on: March 22, 2019
Mapping gas phase dipeptide motions in the far-infrared and terahertz domain
Jérôme Mahé1, Daniël J Bakker, Sander Jaeqx
1LAMBE CNRS UMR8587, Université d'Evry val d'Essonne, Blvd F. Mitterrand, Bât Maupertuis, 91025 Evry, France. mgaigeot@univ-evry.fr.
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.
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