Crystal and molecular structure of cyclo(L-prolyl-glycyl)3: a cyclic hexapeptide with a cis peptide bond

Kartha, G. ; Aimoto, S. ; Varughese, K. I. (1986) Crystal and molecular structure of cyclo(L-prolyl-glycyl)3: a cyclic hexapeptide with a cis peptide bond International Journal of Peptide and Protein Research, 27 (2). pp. 112-117. ISSN 0367-8377

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Official URL: http://www3.interscience.wiley.com/journal/1215797...

Related URL: http://dx.doi.org/10.1111/j.1399-3011.1986.tb01799.x

Abstract

The crystal structure of cyclo(L-Pro-Gly)3 was solved using X-ray crystallographic techniques. The backbone of the peptide is asymmetric and is made up of five trans peptide units and one cis peptide. There is a hydrogen bonded water bridge that links the carbonyl oxygens, O1 and O4. The molecules exist as dimers in the crystal lattice. The two molecules of the dimer are related by crystallographic twofold symmetry and are linked by two N-H O hydrogen bonds. The crystals are trigonal, space group P3212 with a = 11.379(3), c = 32.93(1) and z = 6. The structure was solved by multisolution methods and refined by least squares technique to an R of 0.083.

Item Type:Article
Source:Copyright of this article belongs to Munksgaard International Publishers.
Keywords:Asymmetric Conformation with a Cis Peptide; Cyclic Hexapeptide; X-ray Crystallography
ID Code:28663
Deposited On:15 Dec 2010 11:46
Last Modified:04 Jun 2011 08:48

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