Conformational studies of wheat flour high relative molecular mass glutenin subunits by circular dichroism spectroscopy |
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Authors: | Fisichella S Alberghina G Amato M E Fichera M Mantarro D Palermo A Savarino A Scarlata G |
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Affiliation: | Dipartimento di Scienze Chimiche, Università di Catania, V. le A. Doria 6, 95125 Catania, Italy. sfisichella@dipchi.unict.it |
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Abstract: | Conformational studies of 1Dx2, 1Bx7, and 1Dy12 high relative molecular mass glutenin subunits, extracted from Alisei 1 flour, are reported. Circular dichroism (CD) spectroscopy is employed to study their conformational polymorphism induced by urea and by urea in the presence of 1% sodium dodecyl sulfate (SDS). The CD spectra indicate that SDS promotes ordered structures. The addition of urea to the SDS-acetate solution of 1Dx2, 1Bx7, and 1Dy12 subunits eliminates the effect of SDS. Its addition to the acetate solution of proteins induces conformational transitions to form a poly-L-proline II-like structure. All the changes induced by urea follow a multistep transition process that is typical of proteins consisting of different domains. |
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Keywords: | conformational studies sheat flour relative molecular mass glutenin subunits circular dichroism spectroscopy |
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