Abstract
The secondary structure of prolamins, the storage proteins of wheat (Triticum aestivum L.), rye (Secale cereale L.), and barley (Hordeum vulgare L.), was studied by infrared (IR) spectroscopy. The secondary structure of wheat gliadin was characterized by a high content of unordered conformations of polypeptide chains (64–67%) and a low content of short α-helical regions (4–5%). Elongated conformations, formed by poly-L-proline II helices (61 and 53%) and β-turns (15 and 19%), predominated in rye secalins and barley hordeins. Prolamin proteins of cereal crops also contained β-sheet structure regions comprising 9–12% of the polypeptide chains.
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