期刊
NEW JOURNAL OF CHEMISTRY
卷 27, 期 12, 页码 1789-1793出版社
ROYAL SOC CHEMISTRY
DOI: 10.1039/b305984g
关键词
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The crystal structures of L-Ala-L-Ile, L-Ile-L-Ala, L-Val-L-Val, L-Val-L-Ile and L-Ile-L-Val are presented. Together with L-Ala-L-Val and L-Val-L-Ala they constitute a unique group of seven isostructural dipeptides with hydrophobic pores and identical three-dimensional hydrogen bond networks. Hydrophobic side chains form the inner surfaces of channels parallel to the hexagonal axes in these structures. By changing the bulk of the side chains the van der Waals' diameter of the channels can be regulated within the interval 3.3 to 5.2 Angstrom.
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