Get access

Following the energy transfer in and out of a polyproline–peptide

Authors

  • Wolfgang J. Schreier,

    1. Lehrstuhl für BioMolekulare Optik, Fakultät für Physik and Munich Center for Integrated Protein Science CIPSM, Ludwig-Maximilians-Universität München, Oettingenstr. 67, 80538 München, Germany
    Search for more papers by this author
  • Tobias Aumüller,

    1. Chemistry Department and Munich Center for Integrated Protein Science, TU München, Lichtenbergstrasse 4, 85747 Garching, Germany
    2. Max-Planck-Research Unit for Enzymology of Protein Folding, Weinbergweg 22, 06120 Halle/Saale, Germany
    Search for more papers by this author
  • Karin Haiser,

    1. Lehrstuhl für BioMolekulare Optik, Fakultät für Physik and Munich Center for Integrated Protein Science CIPSM, Ludwig-Maximilians-Universität München, Oettingenstr. 67, 80538 München, Germany
    Search for more papers by this author
  • Florian O. Koller,

    1. Lehrstuhl für BioMolekulare Optik, Fakultät für Physik and Munich Center for Integrated Protein Science CIPSM, Ludwig-Maximilians-Universität München, Oettingenstr. 67, 80538 München, Germany
    Search for more papers by this author
  • Markus Löweneck,

    1. Max-Planck-Institut für Biochemie, Am Klopferspitz 18, 82152 Martinsried, Germany
    Current affiliation:
    1. Senn Chemicals, CH 8157 Dielsdorf, Switzerland
    Search for more papers by this author
  • Hans-Jürgen Musiol,

    1. Max-Planck-Institut für Biochemie, Am Klopferspitz 18, 82152 Martinsried, Germany
    Search for more papers by this author
  • Tobias E. Schrader,

    1. Lehrstuhl für BioMolekulare Optik, Fakultät für Physik and Munich Center for Integrated Protein Science CIPSM, Ludwig-Maximilians-Universität München, Oettingenstr. 67, 80538 München, Germany
    Current affiliation:
    1. Jülich Centre for Neutron Science at FRM II, Forschungszentrum Jülich GmbH, Lichtenbergstr. 1, 85747 Garching, Germany
    Search for more papers by this author
  • Thomas Kiefhaber,

    1. Chemistry Department and Munich Center for Integrated Protein Science, TU München, Lichtenbergstrasse 4, 85747 Garching, Germany
    Search for more papers by this author
  • Luis Moroder,

    1. Max-Planck-Institut für Biochemie, Am Klopferspitz 18, 82152 Martinsried, Germany
    Search for more papers by this author
  • Wolfgang Zinth

    Corresponding author
    1. Lehrstuhl für BioMolekulare Optik, Fakultät für Physik and Munich Center for Integrated Protein Science CIPSM, Ludwig-Maximilians-Universität München, Oettingenstr. 67, 80538 München, Germany
    • Lehrstuhl für BioMolekulare Optik, Fakultät für Physik and Munich Center for Integrated Protein Science CIPSM, Ludwig-Maximilians-Universität München, Oettingenstr. 67, 80538 München, Germany
    Search for more papers by this author

  • This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley. com

Abstract

The intramolecular and intermolecular vibrational energy flow in a polyproline peptide with a total number of nine amino acids in the solvent dimethyl sulfoxide is investigated using time-resolved infrared (IR) spectroscopy. Azobenzene covalently bound to a proline sequence containing nitrophenylalanine as a local sensor for vibrational excess energy serves as a heat source. Information on through-space distances in the polyproline peptides is obtained by independent Förster resonance energy transfer measurements. Photoexcitation of the azobenzene and subsequent internal conversion yield strong vibrational excitation of the molecule acting as a local heat source. The relaxation of excess heat, its transfer along the peptide and to the solvent is monitored by the response of the nitro-group in nitrophenylalanine acting as internal thermometer. After optical excitation, vibrational excess energy is observed via changes in the IR absorption spectra of the peptide. The nitrophenylalanine bands reveal that the vibrational excess energy flows in the peptide over distances of more than 20 Å and arrives delayed by up to 7 ps at the outer positions of the peptide. The vibrational excess energy is transferred to the surrounding solvent on a time scale of 10–20 ps. The experimental observations are analyzed by different heat conduction models. Isotropic heat conduction in three dimensions away from the azobenzene heat source is not able to describe the observations. One-dimensional heat dissipation along the polyproline peptide combined with a slower transversal heat transfer to the solvent surrounding well reproduces the observations. © 2012 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 100: 38–50, 2013.

Get access to the full text of this article

Ancillary