ePrints@IIScePrints@IISc Home | About | Browse | Latest Additions | Advanced Search | Contact | Help

X-ray studies on cyrstalline complexes involving amino acids and peptides. VIII. Head-to-tail arrangement and a specific interaction in the crystal structure of L-arginine acetate

Suresh, CG and Vijayan, M (1983) X-ray studies on cyrstalline complexes involving amino acids and peptides. VIII. Head-to-tail arrangement and a specific interaction in the crystal structure of L-arginine acetate. In: International Journal of Peptide & Protein Research, 21 (3). pp. 223-226.

Full text not available from this repository. (Request a copy)

Abstract

L-Arginine acetate crystallizes in the monoclinic space group P2(1) with a = 9.229(2), b = 5.178(3), c = 13.271(4) A and beta = 111.4(1) degrees. The crystal structure was solved by direct methods and refined to an R value of 0.058 for 1333 observed reflections. The conformation of the arginine molecules in the crystal is different from those observed in the crystals of L-arginine, its salts and complexes. The crystal structure indicates that complexation with a small carboxylic acid like acetic acid is sufficient to align arginine molecules in a head-to-tail fashion. The structure contains a specific ion-pair interaction, involving electrostatic attraction as well as two nearly parallel, N-H ... O hydrogen bonds, between the guanidyl group and the acetate ion.

Item Type: Journal Article
Additional Information: Copyright of this article belongs to Munksgaard International Publishers.
Department/Centre: Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited: 16 Jun 2008
Last Modified: 27 Aug 2008 13:28
URI: http://eprints.iisc.ernet.in/id/eprint/14419

Actions (login required)

View Item View Item