A Molecular Simulation Of Antifreeze Protein Binging To Ice Crastal Plane

A class of proteins known as antifreeze proteins(AFPs)exists in organisms that live in low-temperature environments can absorb to surfaces of ice crystals and lower the temperature at which an ice crystal grows.Ice crystal growth is arrested between the gap of the melting point and the non-equilibrium freezing point of the ice crystal(thermal hysteresis,TH).And it is a non-colligative effect.Experimental evidence supports that AFP molecules can bound to an ice surface and inhibit growth and recrystallization of ice.But it is very difficult to get details of interactions AFP molecules and ice crystal by experimental methods now.This paper use molecular dynamics simulation(MD)to study the fish antifreeze protein(wfAFP)and insect antifreeze protein(sfAFP)interact with water where around the protein in low temperature and the interaction of a spruce budworm antifreeze protein combind with the ice prismatic plane.The results showed that wfAFP and sfAFP can interact with water without conformation changes.At the same time the structure of sfAFP is more stable than wfAFP.And spruce budworm antifreeze protein can be stably combined with prismatic plane to lead the melting of ice.In the process the conformation of sbwAFP is not change.Through such dynamics simulation can helps us to understand more information about antifreeze proteins interact with ice crystal in real system.