Use of neutron scattering techniques for Antifreeze Protein mechanistic studies

Abstract

Antifreeze proteins (AFP) have evolved in organisms living in sub-zero temperatures to avoid freezing of internal fl uids. They bind to ice nuclei lowering the freezing point and inhibiting recrystallization [1]. Even though this protein has been thoroughly studied, including several structures determined by X-ray crystallography, the exact mechanism of binding of ice to the largely hydrophobic Ice Binding Surface (IBS), (i.e. the region of the protein involved in the ice recognition) has remained unclear. In particular, the study of the hydration layers around the protein using X-ray crystallography did not provide a model of the IBS-ice interface.