DSpace
 

RRI Digital Repository >
15. RRI In-House Lectures/Meeting >
Posters >

Please use this identifier to cite or link to this item: http://hdl.handle.net/2289/4740

Title: Molecular dynamics study of a protein-water interface: the role of bound water
Authors: Aishwarya, S.
Rajkamal
Vijayaraghavan, D.
Issue Date: 2011
Citation: RRI In-House Meet, 2011
Abstract: We have calculated the reorientational time correlation function Cμ(t) of water dipoles in the aqueous protein (1ETN) solutions for various protein concentrations at two different temperatures (300 K and 350 K) using atomistic molecular dynamics simulation studies. The reorientational time correlation function follows an exponentially decaying function of the form Cμ(t)=Aexp(-t/τ) , where A represents the percentage of water dipoles reorienting with an average time constant τ. We find that, with increasing protein concentration, the parameter A or the number of freely reorienting dipoles decreases considerably for both temperatures studied and more so at the higher temperature. We infer that this decrease in the number of freely reorientating water molecules may be related to some of the water molecules bound to the protein back bone.
Description: Open Access
URI: http://hdl.handle.net/2289/4740
Copyright: 2011 Raman Research Institute
Appears in Collections:Posters

Files in This Item:

File Description SizeFormat
Vijaraghavan_2011.pdfOpen Access358.89 kBAdobe PDFView/Open

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

 

    RRI Library DSpace