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Interaction of water molecules in non-identical protein structures

Jayalakshmi, J and Mridula, P and Sekar, K and Vaijayanthimala, S and Velmurugan, D (2006) Interaction of water molecules in non-identical protein structures. In: aniIndian Journal of Chemistry Sect. A: Inorgc, Bio-inorganic, Physical, Theoretical & Analytical, 45 (1). pp. 159-162.

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Official URL: http://www.niscair.res.in/sciencecommunication/Res...

Abstract

The interaction of the protein atoms with the surrounding water oxygen atoms has been computed for 392 protein chains from 369 protein structures belonging to 90% non-homologous high resolution (<= 1.5 angstrom) protein Structures with a crystallographic R-factor <= 20%. The percentage composition of the polar atoms is found to be 36.3%. An average of 82.55% of water oxygen atoms are found to be in the primary hydration shell and 15.12% in the secondary hydration shell. The average Percentage of interactions of water oxygen atoms with the polar atoms of the main chain and side chain are 54% and 46%. respectively. The interaction of the acidic residues, aspartate and glutamate, with the water oxygen atoms is more when compared to that of the other residues.

Item Type: Journal Article
Additional Information: Copyright of this article belongs to National Institute of Science Communication and Information Resources.
Department/Centre: Division of Information Sciences > BioInformatics Centre
Division of Information Sciences > Supercomputer Education & Research Centre
Division of Physical & Mathematical Sciences > Physics
Date Deposited: 20 Oct 2010 05:20
Last Modified: 20 Oct 2010 05:20
URI: http://eprints.iisc.ernet.in/id/eprint/32855

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