Conformational studies of wheat flour high relative molecular mass glutenin subunits by circular dichroism spectroscopy.
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.
Fisichella
S
S
Dipartimento di Scienze Chimiche, Università di Catania, V. le A. Doria 6, 95125 Catania, Italy. sfisichella@dipchi.unict.it
Alberghina
G
G
Amato
M E
ME
Fichera
M
M
Mantarro
D
D
Palermo
A
A
Savarino
A
A
Scarlata
G
G
D002942:Circular Dichroism; D005983:Glutens / Q000031:analogs & derivatives* / Q000737:chemistry*; D008970:Molecular Weight; D011487:Protein Conformation / Q000187:drug effects; D021122:Protein Subunits; D012967:Sodium Dodecyl Sulfate / Q000494:pharmacology; D012996:Solutions; D014908:Triticum / Q000737:chemistry*; D014508:Urea / Q000494:pharmacology
D021122:Protein Subunits; D012996:Solutions; D012967:Sodium Dodecyl Sulfate; D005983:Glutens; D014508:Urea; C037302:glutenin