Infrared Spectroscopic Study of the Secondary Structure of Wheat, Rye, and Barley Prolamins

Infrared Spectroscopic Study of the Secondary Structure of Wheat, Rye, and Barley Prolamins 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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Russian Journal of Plant Physiology Springer Journals

Infrared Spectroscopic Study of the Secondary Structure of Wheat, Rye, and Barley Prolamins

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Publisher
Kluwer Academic Publishers-Plenum Publishers
Copyright
Copyright © 2002 by MAIK “Nauka/Interperiodica”
Subject
Life Sciences; Plant Sciences
ISSN
1021-4437
eISSN
1608-3407
D.O.I.
10.1023/A:1015584700841
Publisher site
See Article on Publisher Site

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