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X-ray studies on crystalline complexes involving amino acids and peptides. XII. Peptide aggregation and water structure in the crystals of a hydrated 1:1 complex between L-histidyl-L-serine and glycyl-L-glutamic acid.

Suresh, CG and Vijayan, M (1985) X-ray studies on crystalline complexes involving amino acids and peptides. XII. Peptide aggregation and water structure in the crystals of a hydrated 1:1 complex between L-histidyl-L-serine and glycyl-L-glutamic acid. In: International journal of peptide & protein research, 26 (3). pp. 329-336.

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Abstract

The crystal structure of hexahydrate of a 1:1 complex between L-histidyl-L-serine and glycyl-L-glutamic acid was detd. The two peptide mols. in the structure have somewhat extended conformation. The unlike mols. aggregate into sep. alternating layers. Each layer is stabilized by hydrogen bonded heat-to-tail sequences as well as sequences of hydrogen bonds involving peptide groups. The arrangement of mols. in each layer is similar to one of the plausible idealized arrangements of L-alanyl-L-alanine worked out from simple geometrical considerations. Adjacent layers in the structure and held together by interactions involving side chains as well as water mols. The water structure obsd. in the complex provides a good model, at at. resoln., for that in protein crystals. An interesting feature of the crystal structure is the existence of two water channels in the interfaces between adjacent peptide layers.

Item Type: Journal Article
Additional Information: Copyright belongs to Munksgaard International Publishers Ltd.
Keywords: Organic compounds;Adduct;Dipeptides;Hydrates;Crystalline structure;Molecular structure;X ray diffraction;Experimental study
Department/Centre: Division of Biological Sciences > Molecular Biophysics Unit
Depositing User: RM Shivakumara
Date Deposited: 20 Mar 2008
Last Modified: 27 Aug 2008 13:16
URI: http://eprints.iisc.ac.in/id/eprint/13438

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