Vibrational energy transport in peptide helices after excitation of C-D modes in Leu-d10 (Articolo in rivista)

Type
Label
  • Vibrational energy transport in peptide helices after excitation of C-D modes in Leu-d10 (Articolo in rivista) (literal)
Anno
  • 2009-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1021/jp906363a (literal)
Alternative label
  • Marco Schade; Alessandro Moretto; Marco Crisma; Claudio Toniolo; Peter Hamm (2009)
    Vibrational energy transport in peptide helices after excitation of C-D modes in Leu-d10
    in The journal of physical chemistry. B
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Marco Schade; Alessandro Moretto; Marco Crisma; Claudio Toniolo; Peter Hamm (literal)
Pagina inizio
  • 13393 (literal)
Pagina fine
  • 13397 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#altreInformazioni
  • Citazioni WOS: 20 Impact Factor 2009: 3.471 Coautore (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 113 (literal)
Rivista
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • 1,5: Physikalisch-Chemisches Institut, Universität Zürich, CH-8057 Zürich, Switzerland; 2,3,4: Institute of Biomolecular Chemistry, Padova Unit, CNR, Department of Chemistry, University of Padova, I-35131 Padova, Italy (literal)
Titolo
  • Vibrational energy transport in peptide helices after excitation of C-D modes in Leu-d10 (literal)
Abstract
  • Vibrational energy transport in a short 3(10)-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 do 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) angstrom(2) ps(-1) is the same as that after depositing vibrational energy through the ultrafast internal conversion of a covalently bound chromophore. (literal)
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