With the knowledge of the amino acid sequences of two maize zein proteins (apparent molecular weights of 19,000 and 22,000), a structural model is proposed for their molecular conformation. The circular dichroic spectrum taken in the 190-240 nm range for a zein protein mixture in methanol solution showed the zein secondary structure to be largely helical. The polar, hydrophobic, and turn characteristics of the zein residues, as well as the homologous repeat units in their primary sequences, suggested a structure with nine adjacent, topologically antiparallel helices clustered within a distorted cylinder. Polar residues distributed along the helical surfaces allowed intra- and intermolecular hydrogen bonding such that the zein molecules could be arranged in planes. The proposed glutamine-rich turns located between the helices and at the cylindrical caps would favor side chain interactions resulting in stacking of the molecular planes. Physical properties observed for the zein proteins are explained by the model.