Abstract
Corn, wheat, and soybean seed proteins were examined for potentially useful regularity, size, and polarity. Volume and amphiphilicity profiles evidence analogies to spider silk and human collagen, but seed proteins are 28% larger and 3.6 times more polar per residue. Wheat proteins are more uniform than silk; corn zeins less polar than collagen. A soybean cell wall protein is the most uniform (±5 A 3 ); a corn cell wall peptide is the smallest (92±9 A 3 ) and least polar (2±18) per residue. Selected parts appear to be more useful than whole molecules
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