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Issue 39, 2015
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Can far-IR action spectroscopy combined with BOMD simulations be conformation selective?

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Abstract

The combination of conformation selective far-IR/UV double resonance spectroscopy with Born–Oppenheimer molecular dynamics (BOMD) simulations is presented here for the structural characterization of the Ac-Phe-Pro-NH2 peptide in the far-infrared spectral domain, i.e. for radiation below 800 cm−1. Two conformers have been shown to be present in the experiment, namely a conformer with a γ-turn fold (C7 interaction) and a β-turn fold (C10 interaction). The combined experimental and theoretical work presented here aims to provide spectral features typical of each conformer in this far-IR domain. The simulated BOMD far-IR spectra agree well with the experimental spectra and allow direct assignment of the observed bands. These assignments show that the 400–550 cm−1 spectral domain is conformer selective, allowing us to distinguish the H-bond signature of the γ-turn from the β-turn.

Graphical abstract: Can far-IR action spectroscopy combined with BOMD simulations be conformation selective?

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Publication details

The article was received on 15 Mar 2015, accepted on 26 May 2015 and first published on 26 May 2015


Article type: Paper
DOI: 10.1039/C5CP01518A
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Citation: Phys. Chem. Chem. Phys., 2015,17, 25905-25914
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    Can far-IR action spectroscopy combined with BOMD simulations be conformation selective?

    J. Mahé, S. Jaeqx, A. M. Rijs and M. Gaigeot, Phys. Chem. Chem. Phys., 2015, 17, 25905
    DOI: 10.1039/C5CP01518A

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