## Abstract The highβmolecularβweight glutenin subunits (HMWβGS) of wheat gluten in their native form are incorporated into an intermolecularly disulfideβlinked, polymeric system that gives rise to the elasticity of wheat flour doughs. These protein subunits range in molecular weight from about 70K
β¦ LIBER β¦
Metabolic profiling of transgenic wheat over-expressing the high-molecular-weight Dx5 glutenin subunit
β Scribed by Boryana S. Stamova; Ute Roessner; Suganthi Suren; Debbie Laudencia-Chingcuanco; Antony Bacic; Diane M. Beckles
- Publisher
- Springer
- Year
- 2008
- Tongue
- English
- Weight
- 600 KB
- Volume
- 5
- Category
- Article
- ISSN
- 1573-3882
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This work describes a carbon and proton solid-state NMR study of the hydration of a high molecular weight wheat glutenin subunit, 1Dx5. The effect of the presence of disulfide bonds on the hydration behavior of the subunit is investigated by a comparison of the unalkylated and alkylated forms of the
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