Please use this identifier to cite or link to this item: http://nopr.niscpr.res.in/handle/123456789/19961
Title: Interaction of water molecules in non-identical protein structures
Authors: Jayalakshmi, J
Mridula, P
Sekar, K
Vaijayanthimala, S
Velmurugan, D
Issue Date: Jan-2006
Publisher: NISCAIR-CSIR, India
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 Å) 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.
Page(s): 159-162
ISSN: 0975-0975(Online); 0376-4710(Print)
Appears in Collections: IJC-A Vol.45A(01) [January 2006]

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