Abstract
The peptide Boc-Pro-Hyp-Gly-OMe (I) crystallizes in an orthorhombic system, and was characterized thus: P212121, a = 8.882(1), b = 15.151(2), c = 30.928(4)Å, V = 4162.0(9)Å3, Z = 4. The final R value was 0.0454 for measured reflections. Two peptide molecules were found in the asymmetric unit with a somewhat twisted structure. These molecules were arranged antiparallel, creating a sheet-like structure. A down-pucker was observed for Pro residues, but the both up- and down-puckers were observed for the Hyp residues.
