Document Detail

Following the energy transfer in and out of a polyproline-peptide.
MedLine Citation:
PMID:  23335166     Owner:  NLM     Status:  In-Data-Review    
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.
Wolfgang J Schreier; Tobias Aumüller; Karin Haiser; Florian O Koller; Markus Löweneck; Hans-Jürgen Musiol; Tobias E Schrader; Thomas Kiefhaber; Luis Moroder; Wolfgang Zinth
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Biopolymers     Volume:  100     ISSN:  0006-3525     ISO Abbreviation:  Biopolymers     Publication Date:  2013 Apr 
Date Detail:
Created Date:  2013-01-21     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0372525     Medline TA:  Biopolymers     Country:  United States    
Other Details:
Languages:  eng     Pagination:  38-50     Citation Subset:  IM    
Copyright Information:
Copyright © 2012 Wiley Periodicals, Inc.
Lehrstuhl für BioMolekulare Optik, Fakultät für Physik and Munich Center for Integrated Protein Science CIPSM, Ludwig-Maximilians-Universität München, Oettingenstr. 67, 80538 München, Germany.
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