Glutenin
The glutenins are protein aggregates of high-molecular-mass (HMW) and low-molecular-mass (LMW) subunits with molar masses from about 200,000 to a few million, which are stabilized by intermolecular disulfide bonds, hydrophobic interactions and other forces.Gliadins are monomeric proteins, which can be separated into four groups: alpha-, beta-, gamma- and omega-gliadins.Glutenins occur as multimeric aggregates of high-molecular-mass and low-molecular-mass subunits held together by disulfide bonds.[citation needed] The way the glutenins form their disulfide bond network is predicted to be regulated by the hydrophobicity in the peptide sections where their cysteins are located, explaining why the gliadins are monomeric despite sharing similar conserved cysteine motifs as the LMW-glutenins.[2] Breadmaking qualities are largely dependent on the number and composition of HMW glutenin subunits.