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.Full text not available from this repository.
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|
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