Potential β-Sheet Surfaces of Corn and Wheat Proteins

Comparison of computed profiles for β-sheet conformations of zein, glutelin, gliadin, glutenin, and other cereal or nonplant proteins discloses unusual distributions of volume, polarity, and chemical functionality as well as inter- and intraspecific surface analogies between dissimilar amino acid sequences. Volume and polarity surfaces of major cereal proteins are more like those of collagen or fibrinogen than those of silk or hydrocarbon polymers. Potentially useful segments occur nonrandomly. A low molecular weight glutenin fragment approximates two-thirds of human γ-fibrinogen. Four others duplicate the polarity of 25−50% of collagen. Ten exceptionally asymmetric segments show potential for inclusion in film-forming preparations and adhesives. Ultrahydrophobic sequences in corn oil body oleosins approach the diameter of spider silk, match its uniformity, and exceed its hydrophobicity.