Balasubramanian, Sundaram and Bandyopadhyay, Sanjoy and Pal, Subrata and Bagchi, Biman (2003) Dynamics of water at the interface of a small protein, enterotoxin. In: Current Science (Bangalore), 85 (11). pp. 1571-1578.
Dynamics_of_water.pdf - Published Version
Fully atomistic molecular dynamics simulations have been carried out to investigate the correlation of biological activity with dynamics of water molecules in an aqueous protein solution of the toxic domain of enterotoxin (PDB ID: 1ETN). This is a small protein of 13 amino acid residues. Our study of this water soluble protein clearly reveals that water dynamics slows down in the hydration layer. Despite this general slowing down, water molecules in the vicinity of the second beta turn of this protein exhibit faster dynamics than those near other regions of the protein. Since this beta turn is believed to play a critical role in the receptor binding of this protein, the faster dynamics of water near the beta turn m ay have biological significance. The collective orientational dynamics of the water molecules in the protein solution exhibits a characteristic long time component of 27 ps, which agrees well with dielectric relaxation experiments.
|Item Type:||Journal Article|
|Additional Information:||Copyright of this article belongs to Indian Academy of Sciences.|
|Department/Centre:||Division of Chemical Sciences > Solid State & Structural Chemistry Unit|
|Date Deposited:||19 Aug 2011 07:11|
|Last Modified:||19 Aug 2011 07:11|
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