X-ray studies on crystalline complexes involving amino acids and peptides. X. Head-to-tail sequences in the crystal structure of l-lysine acetate
Article first published online: 12 JAN 2009
© 1983 Munksgaard International Publishers Ltd.
International Journal of Peptide and Protein Research
Volume 22, Issue 5, pages 617–621, November 1983
How to Cite
SURESH, C.G. and VIJAYAN, M. (1983), X-ray studies on crystalline complexes involving amino acids and peptides. X. Head-to-tail sequences in the crystal structure of l-lysine acetate. International Journal of Peptide and Protein Research, 22: 617–621. doi: 10.1111/j.1399-3011.1983.tb02137.x
- Issue published online: 12 JAN 2009
- Article first published online: 12 JAN 2009
- Received 29 December 1982, accepted for publication 22 April 1983
- amino acid conformation;
- head-to-tail arrangement;
- lysine acetate;
- prebiotic polymerisation;
- X-ray crystal structure
l-Lysine acetate crystallises in the monoclinic space group P21 with a = 5.411 (1), b = 7.562(1), c= l2.635(2) Å and β = 91.7(1). The crystal structure was solved by direct methods and refined to an R value of 0.049 using the full matrix least squares method. The conformation and the aggregation of lysine molecules in the structure are similar to those found in the crystal structure of l-lysine l-aspartate. A conspicuous similarity between the crystal structures of l-arginine acetate and l-lysine acetate is that in both cases the strongly basic side chain, although having the largest pK value, interacts with the weakly acidic acetate group leaving the α-amino and the α-carboxylate groups to take part in head-to-tail sequences. These structures thus indicate that electrostatic effects are strongly modulated by other factors so as to give rise to head-to-tail sequences which have earlier been shown to be an almost universal feature of amino acid aggregation in the solid state.