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1 - Proteomics
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Notes
A complete understanding of the basis of wheat quality and wheat quality variation requires an understanding of the molecular structure of gluten proteins and other endosperm components. No gluten protein has yet been crystallized — crystallization would enable exact structure determination by x-ray diffraction approaches. Consequently, we have endeavored to apply computer molecular modeling approaches to prediction of the structure of gluten protein molecules. These approaches to structure prediction included application of force field functions, energy minimization functions, and secondary structure predictions. Shown above are the predicted structures for an α-gliadin peptide, the N-terminal domains of two HMW-glutenin subunits, and a LMW-glutenin subunit (see references for details).
References
Kasarda, D.D. 1997. Gluten and gliadin: precipitating factors in coeliac disease. In: Coeliac Disease:Proceedings of the 7th International Symposium on Coeliac Disease (Eds. M. Maki, P. Collin, and J.K. Visakorpi), September 5-7, 1996, Tampere, Finland; pp.195-212. Published by Coeliac Disease Study Group, Tampere, Finland.
Kasarda, D.D. 1999. Glutenin polymers: The in vitro to in vivo transition. Cereal Foods World 44:566-571. [Size: 3.5 MBytes]
Köhler, P., Keck-Gassenmeier, B., Wieser, H., and Kasarda, D.D. 1997. Molecular modeling of the N-terminal regions of high-molecular-weight glutenin subunits 7 and 5 in relation to intramolecular disulfide bond formation. Cereal Chem. 74:154-158.
Masci, S., D'ovidio, R., Lafiandra, D., and Kasarda, D.D. 1998. Characterization of a low-molecular-weight glutenin subunit gene from bread wheat and the corresponding protein that represents a major subunit of the glutenin polymer. Plant Physiol. 118:1147-1158.
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