Molecular dynamics study of a protein-water interface – The role of bound water

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.