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Vibrational Energy Transport in Peptide Helices after Excitation of C−D Modes in Leu-d10


Schade, M; Moretto, A; Crisma, M; Toniolo, C; Hamm, P (2009). Vibrational Energy Transport in Peptide Helices after Excitation of C−D Modes in Leu-d10. Journal of Physical Chemistry. B, 113(40):13393-13397.

Abstract

Vibrational energy transport in a short 310-helical peptide is studied by time-resolved femtosecond infrared spectroscopy. The C−D vibrations of decadeuterated leucine incorporated in the helical chain are excited, and the subsequent flow of vibrational energy through the helix is monitored by employing C═O probes at various distances from the heat source as local thermometers. The C−D modes are not resonant to the C═O modes, neither directly nor through any Fermi resonance, thereby suppressing resonant energy transfer directly along the C═O oscillators of the peptide backbone. In contrast to our previous work (J. Phys. Chem. B 2008, 112, 9091), we no longer find any substantial difference in the vibrational energy transport efficiency after high- or low-energy excitation. That is, the heat diffusion constant of (2.0 ± 0.5) Å2 ps−1 is the same as that after depositing vibrational energy through the ultrafast internal conversion of a covalently bound chromophore.

Vibrational energy transport in a short 310-helical peptide is studied by time-resolved femtosecond infrared spectroscopy. The C−D vibrations of decadeuterated leucine incorporated in the helical chain are excited, and the subsequent flow of vibrational energy through the helix is monitored by employing C═O probes at various distances from the heat source as local thermometers. The C−D modes are not resonant to the C═O modes, neither directly nor through any Fermi resonance, thereby suppressing resonant energy transfer directly along the C═O oscillators of the peptide backbone. In contrast to our previous work (J. Phys. Chem. B 2008, 112, 9091), we no longer find any substantial difference in the vibrational energy transport efficiency after high- or low-energy excitation. That is, the heat diffusion constant of (2.0 ± 0.5) Å2 ps−1 is the same as that after depositing vibrational energy through the ultrafast internal conversion of a covalently bound chromophore.

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Additional indexing

Item Type:Journal Article, refereed, original work
Communities & Collections:07 Faculty of Science > Department of Chemistry
Dewey Decimal Classification:540 Chemistry
Language:English
Date:15 September 2009
Deposited On:31 Dec 2009 09:44
Last Modified:05 Apr 2016 13:36
Publisher:American Chemical Society
ISSN:1520-5207
Funders:Swiss National Science Foundation (SNF)
Publisher DOI:10.1021/jp906363a
Permanent URL: http://doi.org/10.5167/uzh-24992

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