Ultrafast energy relaxation dynamics of amide I vibrations coupled with protein-bound water molecules
The influence of hydration water on the vibrational energy relaxation in a protein holds the key to understand ultrafast protein dynamics, but its detection is a major challenge. Here, we report measurements on the ultrafast vibrational dynamics of amide I vibrations of proteins at the lipid membran...
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Published in | Nature communications Vol. 10; no. 1; p. 1010 |
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Main Authors | , , , , |
Format | Journal Article |
Language | English |
Published |
London
Nature Publishing Group UK
01.03.2019
Nature Publishing Group Nature Portfolio |
Subjects | |
Online Access | Get full text |
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Summary: | The influence of hydration water on the vibrational energy relaxation in a protein holds the key to understand ultrafast protein dynamics, but its detection is a major challenge. Here, we report measurements on the ultrafast vibrational dynamics of amide I vibrations of proteins at the lipid membrane/H
2
O interface using femtosecond time-resolved sum frequency generation vibrational spectroscopy. We find that the relaxation time of the amide I mode shows a very strong dependence on the H
2
O exposure, but not on the D
2
O exposure. This observation indicates that the exposure of amide I bond to H
2
O opens up a resonant relaxation channel and facilitates direct resonant vibrational energy transfer from the amide I mode to the H
2
O bending mode. The protein backbone motions can thus be energetically coupled with protein-bound water molecules. Our findings highlight the influence of H
2
O on the ultrafast structure dynamics of proteins.
Vibrational energy relaxation of proteins helps us to understand ultrafast protein dynamics. Here, the authors determine the vibrational energy transfer time of the amide I mode in aqueous environment and find that water provides a “shortcut” through a direct resonant channel to dissipate energy into the solvent. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 2041-1723 2041-1723 |
DOI: | 10.1038/s41467-019-08899-3 |