Abstract
Small angle X-ray scattering in solution was performed on seed-storage proteins from wheat. Three different groups of gliadins (α-, γ- and ω-) and a high molecular weight (HMW) subunit of glutenin (1Bx20) were studied to determine molecular size parameters. All the gliadins could be modelled as prolate ellipsoids with extended conformations. The HMW subunit existed as a highly extended rod-like particle in solution with a length of about 69 nm and a diameter of about 6.4 nm. Specific aggregation effects were observed which may reflect mechanisms of self-assembly that contribute to the unique viscoelastic properties of wheat dough. Copyright (C) 1999 Elsevier Science B.V.
Original language | English |
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Pages (from-to) | 359-366 |
Number of pages | 8 |
Journal | Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular |
Volume | 1430 |
Issue number | 2 |
DOIs | |
Publication status | Published - 19 Mar 1999 |
Externally published | Yes |
Keywords
- Gliadin
- Glutenin
- Small angle X-ray scattering