Dalhus B, Görbitz C H
Department of Chemistry, University of Oslo, Blindern, Norway.
Acta Crystallogr C. 1996 Aug 15;52 ( Pt 8):2087-90. doi: 10.1107/s0108270196002041.
The asymmetric unit (C17H25N3O5.C3H8O.2H2O) consists of two crystallographically independent peptide molecules, A and B, with different conformations, chi 1(2) being trans and gauche- for the Leu residues in molecules A and B, respectively. The backbone conformation of both peptide molecules resembles that of the beta-pleated sheet arrangement found in proteins. Comparison with two other structures containing the tripeptide Gly-L-Leu-L-Tyr reveals almost identical molecular conformations, and in one instance also a common packing pattern.
不对称单元（C17H25N3O5.C3H8O.2H2O）由两个晶体学独立的肽分子A和B组成，它们具有不同的构象，分子A和B中亮氨酸残基的χ1(2)分别为反式和顺式。两个肽分子的主链构象类似于蛋白质中发现的β-折叠片层排列。与另外两个含有三肽甘氨酸-L-亮氨酸-L-酪氨酸的结构比较，发现分子构象几乎相同，在一个实例中还具有共同的堆积模式。
