Solution conformational analysis of the α-zein proteins of maize

Small angle x-ray scattering and viscometric analyses of the α-zeins of maize in solution indicated that the molecules were asymmetric. Structure predictions of consensus sequences for the two classes of α-zeins, Z19 and Z22, were in good agreement with the α-helical contents determined by circular dichroism. Dimensions determined by small angle x-ray scattering and viscometry indicated a predominantly α-helical conformation. The data are discussed in relation to models for the solution conformation and to earlier models for α-zeins structure.