Alanyl side chain folding in phenylalanine: Conformational assignments through ultraviolet rotational band contour analysis

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Partially resolved ultraviolet rotational band contours associated with the S-1 <-- S-0 origin bands of the six most populated conformers of jet-cooled phenylalanine have been recorded via resonant two-photon ionization. The strong dependence of their transition moment orientation on the conformation of the alanyl side chain has facilitated their structural assignment through simulations based upon ab initio computation. The S-1 lifetimes of all six conformers, measured through pump-probe delayed ionization, reveal an efficient nonradiative decay pathway in the most stable conformer, which is stabilized through a chain of intramolecular hydrogen bonds linking the side chain to the benzene ring.
Publisher
AMER CHEMICAL SOC
Issue Date
2004-01
Language
English
Article Type
Article
Keywords

ION-DIP SPECTROSCOPY; AMINO-ACIDS; GAS-PHASE; DEPENDENT IONIZATION; TRANSITION-MOMENT; HYDRATED CLUSTERS; SUPERSONIC JET; BIOMOLECULES; LANDSCAPES; WATER

Citation

JOURNAL OF PHYSICAL CHEMISTRY A, v.108, no.1, pp.69 - 73

ISSN
1089-5639
DOI
10.1021/jp0368280
URI
http://hdl.handle.net/10203/83495
Appears in Collection
CH-Journal Papers(저널논문)
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