Structural Flexibility of a Helical Peptide Regulates Vibrational Energy Transport Properties

Applying ultrafast vibrational spectroscopy, we find that vibrational energy transport along a helical peptide changes from inefficient but mostly ballistic below ≈270 K into diffusive and significantly more efficient above. On the basis of molecular dynamics simulations, we attribute this change to...

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Bibliographic Details
Published in:The journal of physical chemistry. B 2008-12, Vol.112 (48), p.15487-15492
Main Authors: Backus, Ellen H. G, Nguyen, Phuong H, Botan, Virgiliu, Moretto, Alessandro, Crisma, Marco, Toniolo, Claudio, Zerbe, Oliver, Stock, Gerhard, Hamm, Peter
Format: Article
Language:English
Subjects:
B: Biophysical Chemistry
Computer Simulation
Crystallography, X-Ray
Deuterium
Energy Transfer
Peptides - chemistry
Protein Conformation
Spectrophotometry, Infrared
Spectrophotometry, Ultraviolet
Spectroscopy, Fourier Transform Infrared
Temperature
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Summary:Applying ultrafast vibrational spectroscopy, we find that vibrational energy transport along a helical peptide changes from inefficient but mostly ballistic below ≈270 K into diffusive and significantly more efficient above. On the basis of molecular dynamics simulations, we attribute this change to the increasing flexibility of the helix above this temperature, similar to the glass transition in proteins. Structural flexibility enhances intramolecular vibrational energy redistribution, thereby refeeding energy into the few vibrational modes that delocalize over large parts of the structure and therefore transport energy efficiently. The paper outlines concepts how one might regulate vibrational energy transport properties in ultrafast photobiological processes, as well as in molecular electronic devices, by engineering the flexibility of their components.
ISSN:1520-6106
1520-5207
DOI:10.1021/jp806403p