Please use this identifier to cite or link to this item:
Title: Molecular dynamics study of a protein-water interface – The role of bound water
Authors: Aishwarya, S.
Vijayaraghavan, D.
Issue Date: Oct-2012
Publisher: Excel (India) Publishers, New Delhi
Citation: Proceedings of International Conference on Research in Condensed Matter Physics, held at University of Madras, Chennai, India, October 2012, :Dr. Rita John & Dr. Tamio Endo; p 227-229
Abstract: We have calculated the reorientational time correlation function Cµ(t) of water dipoles in the aqueous. protein (lETN)) solution 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 functions of the form Cµ(t)=Aexp(-1-π), where A represents the percentage of water dipoles reorienting with increasing proteins concentration , the parameter A or the number of freely reorienting dipoles decreases considerably for both temperatures studies and more so at thr higher temperatures . We infer that this decreases the number of freely reorienting water molecules may be related to some of the water molecule bound to the protein back bone.
Description: Restricted Access.
ISBN: 9789382062639
Copyright: Excel (India) Publishers
Appears in Collections:Research Papers (SCM)

Files in This Item:
File Description SizeFormat 
  Restricted Access
Restricted Access499.96 kBAdobe PDFView/Open Request a copy

Items in RRI Digital Repository are protected by copyright, with all rights reserved, unless otherwise indicated.