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首页> 外文期刊>Acta Crystallographica Section E: Crystallographic Communications >Crystal structure of the tripeptide N-(benzyl­oxycarbon­yl)glycylglycyl-l-norvaline
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Crystal structure of the tripeptide N-(benzyl­oxycarbon­yl)glycylglycyl-l-norvaline

机译:三肽N-(苄氧羰基)甘氨酰甘氨酰基-1-正缬氨酸的晶体结构

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摘要

The title tripeptide, C17H23N3O6, contains a nonproteinogenic C-terminal amino acid residue, norvaline, which is an isomer of the amino acid valine. Norvaline, unlike valine, has an unbranched side chain. The mol­ecule has a Gly–Gly segment which adopts an extended conformation. The norvaline residue also adopts an extended backbone conformation while its side chain has a g+t conformation. In the crystal lattice, N—H⋯O and O—H⋯O hydrogen bonds stabilize the packing. Mol­ecules translated along the crystallographic a axis associate through an N—H⋯O hydrogen bond. The remaining three hydrogen bonds are between mol­ecules related by a 21 screw axis.
机译:标题三肽C17H23N3O6包含一个非蛋白质的C端氨基酸残基正缬氨酸,它是氨基酸缬氨酸的异构体。与缬氨酸不同,Norvaline具有未分支的侧链。该分子具有一个Gly-Gly区段,该区段采用扩展的构象。正缬氨酸残基还具有扩展的骨架构象,而其侧链具有g + t构象。在晶格中,NH-OH和OH-O氢键稳定了堆积。沿结晶轴平移的分子通过N-H = O氢键缔合。其余三个氢键位于21螺旋轴相关的分子之间。

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