Conformational landscapes in amino acids: infrared and ultraviolet ion-dip spectroscopy of phenylalanine in the gas phase
Conformational landscapes in amino acids: infrared and ultraviolet ion-dip spectroscopy of phenylalanine in the gas phase
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DOI：
10.1016/s0009-2614(00)00320-1
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发表时间：
2000-04-21
影响因子：
2.8
通讯作者：
Simons, JP
中科院分区：
文献类型：
--
作者：
Snoek, LC;Robertson, EG;Simons, JP
苯丙氨酸的最稳定的构象，结合紫外和红外离子浸渍光谱的喷射冷却的氨基酸，再加上高层次的从头计算的基础上，提出了一个完整的结构分配的第一次。结果进行了讨论，在脂肪族氨基酸突出环侧链相互作用的重要性，也讨论了两性形成的问题。(C)2000 Elsevier Science B.V.保留所有权利。
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.