Journal
PHYSICAL CHEMISTRY CHEMICAL PHYSICS
Volume 17, Issue 39, Pages 25905-25914Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c5cp01518a
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Funding
- GENCI-France [072484]
- Nederlandse Organisatie voor Wetenschappelijk Onderzoek (NWO)
- NWO BIG-programme
- NWO Physical Sciences (EW)
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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 gamma-turn fold (C7 interaction) and a beta-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 gamma-turn from the beta-turn.
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