Crystal structure and conformational analyses of a synthetic tetrapeptide t-Boc-L-Val-Aib-Gly-L-Leu-OMe by Ravindranath Singh Rathore

Crystal Research and Technology

Cryst. Res. Technol. 40, 627 (2005) - Abstract -

Crystal structure and conformational analyses of a synthetic tetrapeptide t-Boc-L-Val-Aib-Gly-L-Leu-OMe

Ravindranath Singh Rathore

Department of Physics, Indian Institute of Science, Bangalore, Karnataka, 560 012, India

Keywords	de novo peptide design, tetra peptide, Aib, water-peptide interactions
PACS	87.15.-v
DOI	10.1002/crat.200410394

Crystal structure of a terminally blocked synthetic peptide, t-Boc-L-Val-Aib-Gly-L-Leu-OMe has been investigated. Two different conformers of peptide with one co-crystallized water molecule, coexist in the crystal structure, in C2 space group. Both the conformers are stabilized by two intramolecular 1<-4 hydrogen bonds, between (Boc) C=O ^... HN (Gly) and (Val) C=O ^... HN (Leu), forming consecutive type II-I' β-turns. In the crystal, water interlinks peptide molecules, making a triangular bridge of pyramidal type.

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