Crystal structure of the tripeptide N-(benzyl­oxycarbon­yl)glycylglycyl-l-norvaline

Acta Crystallographica Section E: Crystallographic Communications

Nicholas, S.¹ 

[1] Dept. of Physics, Indian Institute of Science, Bangalore 560012, India

关键词: CRYSTAL STRUCTURE;    PEPTIDE;    CONFORMATION;    NORVALINE;    GLYCINE;    HYDROGEN BONDING;   

DOI  :  10.1107/S205698901500393X

学科分类：数学（综合）

来源: International Union of Crystallography

【 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.

【 授权许可】

CC BY