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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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 |
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Publication: | aniIndian Journal of Chemistry Sect. A: Inorgc, Bio-inorganic, Physical, Theoretical & Analytical |
Publisher: | National Institute of Science Communication and Information Resources |
Additional Information: | Copyright of this article belongs to National Institute of Science Communication and Information Resources. |
Department/Centre: | Division of Information Sciences (Doesn't exist now) > BioInformatics Centre Division of Interdisciplinary 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.ac.in/id/eprint/32855 |
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