四肽Z-亮氨酸-氨基异丁酸-脯氨酸-缬氨酸-OBg一水合物
The tetrapeptide Z-Leu-Aib-Pro-Val-OBg monohydrate.
作者信息
Gessmann Renate, Schiemann Norbert, Brückner Hans, Petratos Kyriacos
机构信息
IMBB/FORTH, PO Box 1527, 71110 Iraklion, Crete, Greece.
出版信息
Acta Crystallogr C. 2003 Aug;59(Pt 8):o413-5. doi: 10.1107/s0108270103010291. Epub 2003 Jul 12.
The intramolecular hydrogen-bonding pattern of Z-Leu-Aib-Pro-Val-OBg monohydrate [(N-benzhydrylamino)carbonylmethyl N-benzyloxycarbonyl-alpha-aminoisobutyrylprolylvalinate monohydrate], C(43)H(55)N(5)O(8).H(2)O, is unusual for a tetrapeptide because, in addition to a 1-->4 hydrogen bond, a second hydrogen bond of the type 1-->5 is formed. This folding reflects the intramolecular hydrogen-bonding pattern that this amino acid sequence adopts in the naturally occurring peptaibol alamethicin.
Z-亮氨酸-氨基异丁酸-脯氨酸-缬氨酸-OBg一水合物[（N-二苯甲基氨基）羰基甲基N-苄氧羰基-α-氨基异丁酰基脯氨酰缬氨酸一水合物]，化学式为C(43)H(55)N(5)O(8).H(2)O，其分子内氢键模式对于四肽而言是不寻常的，因为除了1→4氢键外，还形成了第二种1→5型氢键。这种折叠反映了该氨基酸序列在天然存在的肽抗生素短杆菌肽A中所采用的分子内氢键模式。
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