Computer Simulations Reveal How Anti-Freeze Proteins Work

Summary

Research lead by Jeremy Smith of Oak Ridge National Laboratory (ORNL) has yielded new insight into the mechanism of how anti-freeze proteins, found in a wide range of organisms, prevent ice formation.  Utilizing the high performance computational resources at ORNL, the molecular dynamics simulations reveal that at lower temperatures the anti-freeze protein serves a dual purpose: preconfiguring the water to ease ice binding to one face of the protein while disordering the water on the other faces to prevent ice propagation.  ORNL researchers term the preconfiguration effect “pre-ordering-binding” and suggest that the mechanism may be generally applicable to processes occurring at disordered or amorphous surfaces.  A similar simulation approach is planned to examine water structure in lignocellulosic biomass, as similar hydration effects may form a barrier to cellulosic ethanol production.  This work is sponsored in part by DOE’s Office of Science.  Details can be found in the October issue of the J.  Am.  Chem.  Soc., 130 (39), 13066-13073, 2008.  The article was featured as a Research Highlight in the September 2008 edition of Nature Chemistry.