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Conformational studies of wheat flour high relative molecular mass glutenin subunits by circular dichroism spectroscopy
Author(s) -
Fisichella S.,
Alberghina G.,
Amato M. E.,
Fichera M.,
Mantarro D.,
Palermo A.,
Savarino A.,
Scarlata G.
Publication year - 2002
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.10211
Subject(s) - chemistry , glutenin , circular dichroism , urea , sodium dodecyl sulfate , molecular mass , crystallography , conformational change , protein subunit , chromatography , stereochemistry , biochemistry , enzyme , gene
Conformational studies of 1D x 2, 1B x 7, and 1D y 12 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 1D x 2, 1B x 7, and 1D y 12 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. © 2002 Wiley Periodicals, Inc. Biopolymers (Biospectroscopy) 65: 142–147, 2002