Arthur S. Tatham

TL;DR: All storage protein fractions are mixtures of components that exhibit polymorphism both within single genotypes and among genotypes of the same species, which arises from the presence of multigene families and, in some cases, proteolytic processing and glycosylation.

TL;DR: The high molecular weight subunits of wheat glutenin are of considerable interest because of their relationship to breadmaking quality and how they may be assembled to form disulphide-bonded polymers that confer elasticity on wheat dough.

TL;DR: The prolamins of wheat, barley and maize have been studied in detail at the molecular and physicochemical levels, and these will be focused on.

TL;DR: Direct disulphide bond determination demonstrates that the conserved cysteine residues present in S-rich prolamins (α- type gliadins, γ-type gliADins and LMW subunits) form intra-chain disULphide bonds while additional cysteines residues present only in the L MW subunits form inter-chain bonds with cysteins in HMW sub units and other LMWSubunits.

TL;DR: The wheat gluten proteins correspond to the major storage proteins that are deposited in the starchy endosperm cells of the developing grain and are brought together to form a continuous viscoelastic network when flour is mixed with water to form dough.