期刊
CHEMICAL PHYSICS LETTERS
卷 321, 期 1-2, 页码 49-56出版社
ELSEVIER
DOI: 10.1016/S0009-2614(00)00320-1
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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. (C) 2000 Elsevier Science B.V. All rights reserved.
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