Conformational landscapes in amino acids: infrared and ultraviolet ion-dip spectroscopy of phenylalanine in the gas phase

A full structural assignment of the most stable conformers of phenylalanine, based upon a combination of ultraviolet and infrared ion-dip spectroscopy of the jet-cooled amino acid, coupled with high-level ab initio computation is presented for the first time. The results are discussed in relation to...

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Bibliographic Details
Published in:Chemical physics letters 2000-04, Vol.321 (1), p.49-56
Main Authors: Snoek, L.C, Robertson, E.G, Kroemer, R.T, Simons, J.P
Format: Article
Language:English
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Summary:A full structural assignment of the most stable conformers of phenylalanine, based upon a combination of ultraviolet and infrared ion-dip spectroscopy of the jet-cooled amino acid, coupled with high-level ab initio computation is presented for the first time. The results are discussed in relation to aliphatic amino acids to highlight the importance of ring–side chain interactions; the question of zwitterion formation is also discussed.
ISSN:0009-2614
1873-4448
DOI:10.1016/S0009-2614(00)00320-1