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research article

Conformation-specific spectroscopy and photodissociation of cold, protonated tyrosine and phenylalanine

Stearns, Jaime A.
•
Mercier, Sébastien
•
Seaiby, Caroline  
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2007
Journal of the American Chemical Society

We present here ultraviolet and infrared spectra of protonated aromatic amino acids in a cold, 22-pole ion trap. Ultraviolet photofragmentation spectra of protonated tyrosine and phenylalanine show vibronically resolved bands corresponding to different stable conformers: two for PheH+ and four in the case of TyrH+. We subsequently use the resolved UV spectra to perform conformer-specific infrared depletion spectroscopy. Comparison of the measured infrared spectra to density functional theory calculations helps assign the geometry of the various conformers, all of which exhibit NH3-π hydrogen bonds and NH3-O=C interactions, with the COOH group oriented either anti or gauche to the aromatic ring. In both molecules the majority of the observed fragments result from dissociation on an excited electronic state. In TyrH+, different conformers excited with practically the same energy exhibit different fragmentation patterns, suggesting that the excited-state dynamics depends upon conformation.

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Type
research article
DOI
10.1021/ja0736010
Web of Science ID

WOS:000249693800031

Author(s)
Stearns, Jaime A.
Mercier, Sébastien
Seaiby, Caroline  
Guidi, Monia
Boyarkin, Oleg V.  
Rizzo, Thomas R.  
Date Issued

2007

Published in
Journal of the American Chemical Society
Volume

129

Article Number

11814

Subjects

biomolecules

•

spectrocopy

•

double resonance

Editorial or Peer reviewed

REVIEWED

Written at

EPFL

EPFL units
LCPM  
Available on Infoscience
May 21, 2007
Use this identifier to reference this record
https://infoscience.epfl.ch/handle/20.500.14299/7013
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