Seed protein topology: molecular profiles
1994
Rothfus, J.A. | Hagemann, J.W.
Corn, wheat, and soybean seed proteins were esamined 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 angsroms3); a corn cell wall peptide is the smallest (92 +/- 9 angstroms3) and least polar (2 +/- 18) per residue. Selected parts appear to be more useful than whole molecules. The alpha subunit of soybean beta- conglycinin concentrates half its acidic residues in the N-terminal third of the molecule and 90% of its hydrophobic residues in the remainder. Corn glutelin and wheat gliadins contain lengthy (7.6-16.3 kDa) repetitive segments. Signal peptides share similar volumes with the proteins but are more than twice as hydrophobic.
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