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X-Ray Studies On Crystalline Complexes Involving Amino-Acids And Peptides .11. 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 .11. 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 and Protein Research, 26 (3). 329 -336.

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Official URL: http://www3.interscience.wiley.com/journal/1214996...

Abstract

The hexahydrate of a 1:1 complex between L-histidyl-L-serine and glycyl-L-glutamic acid crystallizes in space group P1 with a = 4.706(1), b= 8.578(2), c= 16.521(3) ÅA; α= 85.9(1), β= 89.7(1)°, = 77.4(1). The crystal structure, solved by direct methods, has been refined to an R value of 0.046 for 2150 observed reflections. The two peptide molecules in the structure have somewhat extended conformations. The unlike molecules aggregate into separate alternating layers. Each layer is stabilized by hydrogen bonded head-to-tail sequences as well as sequences of hydrogen bonds involving peptide groups. The arrangement of molecules 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 are held together by interactions involving side chains as well as water molecules. The water structure observed in the complex provides a good model, at atomic resolution, 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 of this article belongs to Wiley.
Keywords: head-to-tail sequence • peptide aggregation • peptide complex • peptide-water interactions • water structure • X-ray crystal structure
Department/Centre: Division of Biological Sciences > Molecular Biophysics Unit
Depositing User: Paramesha S
Date Deposited: 02 Feb 2010 08:11
Last Modified: 02 Feb 2010 08:11
URI: http://eprints.iisc.ac.in/id/eprint/22972

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