Gliadins composition

H Wieser, A Modi, W Seilmeier, HD Belitz. High-performance liquid chromatography of gliadins from different wheat varieties amino acid composition and N-terminal amino acid sequence of components. Z Lebensm Unters Forsch 185 371-378, 1987. 

Daniel, C. and Triboi, E. 2000. Effects of temperature and nitrogen nutrition on the grain composition of winter wheat Effects of gliadin content and composition. J Cereal Sci 32(1) 45-56. 

Cornell HJ. Amino acid composition of peptides remaining after in vitro digestion of a gliadin sub-fraction with duodenal mucosa from patients with coeliac disease. Clin Chim... 

From the unique amino acid composition of the gliadin proteins, one would expect a structure that is quite different from globular proteins. However, optical rotation studies have shown that the gliadin proteins possess compact tertiary structures similar to those of globular proteins (4,5). 

Dietary protein sources differ widely in their proportions of the EAA. In general, complete proteins (those containing sufficient quantities of EAA) are of animal origin (e.g., meat, milk, and eggs). Plant proteins often lack one or more EAA. For example, gliadin (wheat protein) has insufficient amounts of lysine, and zein (com protein) is low in both lysine and tryptophan. Because plant proteins differ in their amino acid compositions, plant foods can provide a high-quality source of essential amino acids only if they are eaten in appropriate combinations. One such combination includes beans (low in methionine) and cereal grains (low in lysine). 

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