Investigations of structure and dynamics of water solvation of the type I antifreeze protein

Abstract

AbstractWe use molecular dynamics simulations to study the water structure and dynamics around the winter flounder antifreeze protein (AFP) and its two mutant forms in which the four key threonine residues of the winter flounder AFP are mutated to alanines and serines, respectively. The TIP4P‐Ew water model is used to better describe the water interactions and water structure; all simulations are performed at 245.5 K, a temperature near the freezing point of the TIP4P‐Ew water model. Analysis of structural and dynamic properties of the water around the threonines in the winter flounder AFP reveals that the water structure is ordered around the threonine residues, especially in the second‐solvation shell. Alanine and serine mutations instead promote water hydration in the first‐solvation shell. Also our calculations show that in the close vicinity of the threonine residues of the wild‐type AFP, the mobility of water molecules is substantially decreased. A smaller effect is observed for the weakly active alanine‐substituted mutant, and no effect is observed for the inactive serine‐substituted mutant. The results of this study suggest that water ordering and immobilization play important roles in the recognition and adsorption of the antifreeze protein to ice. © 2008 Wiley Periodicals, Inc. Int J Quantum Chem, 2009