Hemant, Yennawar P and Viswamitra, MA (1989) Crystal structure of L-lysyl-L-glutamic acid dihydrate. In: International Journal of Peptide & Protein Research, 34 (1). pp. 42-45.Full text not available from this repository.
L-Lysyl-L-glutamic acid dihydrate, C11N3O5H21·2H2O, crystallizes in the monoclinic space group P21 with a = 12.474(2), b = 5.020(1), c = 13.157(2) Å, β= 114.69(1)° and Z = 2. The crystal structure was solved by direct methods and refined to an R value of 0.037 using full matrix least-squares method. The molecule exists as a double zwitterion with both the amino and carboxyl groups ionised. The peptide has a folded conformation with its Lys residue trans and Glu residue gauche−gauche+. The side chains of the Lys and Glu residues correspond to all trans and folded (g−g−g−) conformations respectively. The terminal carboxyl group forms hydrogen bonds with the ξ-amino group of the lysine side chain. The head-to-tail interaction often seen in peptide crystals is absent in the present structure. In the extended crystal structure water molecules form channels along the b direction and are enclosed within helically arranged hydrogen bonds formed by the lysine side chain and the peptide backbone.
|Item Type:||Journal Article|
|Additional Information:||Copyright of this article belongs to John Wiley and Sons.|
|Keywords:||L-Lys-L-Glu;peptide aggregation;peptide conformation;X-ray crystal structure.|
|Department/Centre:||Division of Physical & Mathematical Sciences > Physics
Division of Biological Sciences > Microbiology & Cell Biology
|Date Deposited:||13 Aug 2010 09:32|
|Last Modified:||13 Aug 2010 09:32|
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