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GrainGenes Reference Report: BPY-65-142

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Reference	BPY-65-142
Title	Conformational studies of wheat flour high relative molecular mass glutenin subunits by circular dichroism spectroscopy
Journal	Biopolymers
Year	2002
Volume	65
Pages	142-147
Author	Fisichella S [ Show all 8 ]
Abstract	Summary: Conformational studies of 1Dx2, 1Bx7, and 1Dgamma12 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 1Dgamma12 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
External Databases	Pubmed: 12209464
Keyword	[ Hide all but 1 of 29 ] acetate addition biochemistry biophysics cd cd spectrum circular dichroism circular dichroism spectroscopy conformational studies flour follow gel-electrophoresis glutenin molecular mass pepsinogen polymorphism relative molecular mass sds seed storage protein sheat flour sodium sodium dodecyl sulfate spectroscopy spectrum structure subunit sulfate transition urea

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