1 Contains
| DB identifier | Type | Name |
|---|---|---|
| IPR016140 | Domain | Bifunctional inhibitor/plant lipid transfer protein/seed storage helical domain |
| Type: | Family | Name: | HMW glutenin |
| Description: | Gluten is the protein component of wheat flour. It consists of numerous proteins, which are of two different types responsible for different physicalproperties of dough: the glutenins, which are primarily responsible for the elasticity, and the gliadins, which contribute to the extensibility.The glutenins are of two different types, termed low (LMW) and high molecular weight (HMW) subunits []. The glutenin high molecular weight subunits are classified aselastomeric proteins, because the glutenin network can withstand significant deformations without breaking, and return to the original conformation when the stress is removed. Elastomeric proteins differ considerably in amino acid sequence, but they are allpolymers whose subunits consist of elastomeric domains, composed of repeated motifs, and non-elastic domains that mediate cross-linking between the subunits. The elastomeric domain motifs are all rich in glycine residues in addition to other hydrophobicresidues. High molecular weight glutenin subunits have an extensive central elastomeric domain, flanked by two terminal non-elastic domains that form disulphide cross-links. The central elastomeric domain is characterised by the following three repeated motifs:PGQGQQ, GYYPTS[P/L]QQ, GQQ. It possesses overlapping beta-turns within and between the repeated motifs, and assumes aregular helical secondary structure with a diameter of approx. 1.9 nm and a pitch of approx. 1.5 nm []. | Short Name: | Glutenin |
| DB identifier | Type | Name |
|---|---|---|
| IPR016140 | Domain | Bifunctional inhibitor/plant lipid transfer protein/seed storage helical domain |
