Dynamics of water at the interface of a small protein, enterotoxin

Abstract

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 b turn of this protein exhibit faster dynamics than those near other regions of the protein. Since this β turn is believed to play a critical role in the receptor binding of this protein, the faster dynamics of water near the β turn may 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.