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. (Request a copy)Abstract
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 |
|---|---|
| Publication: | International Journal of Peptide & Protein Research |
| Publisher: | John Wiley and Sons |
| 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 |
| URI: | http://eprints.iisc.ac.in/id/eprint/31266 |
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