Solution conformational analysis of the alpha-zein proteins of maize.

Abstract

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