Crystal structure of the tripeptide N-(benzyl-oxycarbon-yl)glycylglycyl-l-norvaline.

ABSTRACT: 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 mol-ecule 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. Mol-ecules translated along the crystallographic a axis associate through an N-H⋯O hydrogen bond. The remaining three hydrogen bonds are between mol-ecules related by a 2 1 screw axis.

SUBMITTER: Nicholas S 

PROVIDER: S-EPMC4350747 | biostudies-literature | 2015 Mar

REPOSITORIES: biostudies-literature