Antifreeze proteins (AFPs) designate a class of proteins that are able tobind toand inhibit the growthofmacromolecular ice. These proteins have been characterized froma variety of organisms. Recently, the structures ofAFPs fromthe spruce budworm (Choristoneura fumiferana) and the yellow meal-worm (Tenebrio molitor) have been determined by NMR and X-ray crystallography. Despite nonhomologous sequences, both proteins were shown to consist ofb-helices. We review the structures and dynamics data of these two insect AFPs to bring insight into the structure–function relationship and explore theirb-helical architecture
