1 Contains
| DB identifier | Type | Name |
|---|---|---|
| IPR013771 | Domain | Bifunctional trypsin/alpha-amylase inhibitor helical domain |
| Type: | Family | Name: | Gliadin, alpha/beta |
| Description: | Gluten is the protein component of Triticum aestivum(Wheat) flour. It consists of numerous proteins, which are of 2 different types responsible for different physical properties of dough: the glutenins, which are primarily responsible for the elasticity, and the gliadins, which contribute to the extensibility. The glutenins themselves are of 2 different types, termed low and high [] molecular weight subunits. The latter have unusual structures: a central region contains multiple tandem repeats of blocks of amino acids, forming a loose helix based on beta reverse turns, and is flanked by globular regions, which can be cross-linked by disulphide bonds. The result is an elastic network in which the elasticity may derive from the cross-linking, the helical structure, or a combination of these [].The gliadins are also of different types (e.g., alpha/beta or gamma) and, like the glutenins, contain repetitive sequences [] that form loose helical structures, but are usually associated with more extensive non-repetitive regions, which are compact and globular [].Gliadins are a complex mixture of proteins that contain at least 40 different components in a single variety of wheat. The alpha/beta gliadins can be divided into five homology classes. Sequence divergence between the classes is due to single base substitutions and to duplications or deletions within or near direct repeats []. | Short Name: | Gliadin |
| DB identifier | Type | Name |
|---|---|---|
| IPR013771 | Domain | Bifunctional trypsin/alpha-amylase inhibitor helical domain |
