The formation of the large protein structure known as "gluten" during dough-mixing and bread-making processes is extremely complex. It has been established that a specific subset of the proteins comprising gluten, the glutenin subunits, directly affects dough formation and breadmaking quality. Glutenin subunits have no definitive structural differences that can be directly correlated to their a...

Certain disulfide bonds present in leucocyte membrane proteins are labile and can be reduced in inflammation. This can cause structural changes that result in downstream functional effects, for example, in integrin activation. Recent studies have shown that a wide range of membrane proteins have labile disulfide bonds including CD132, the common gamma chain of the receptors for several cytokine...

The ionizing radiation sensitivity of ricin, a disulfide-linked heterodimeric protein, was studied as a model to determine the ability of disulfide bonds to transmit destructive energy. The radiation-dependent loss of A chain enzymatic activity after irradiation of either intact ricin or ricin in which the interchain disulfide bond was disrupted gave target sizes corresponding to the molecular ...

The availability of stable, purified preparations of bovine pancreatic deoxyribonuclease (mol wt 31,000) has prompted study of the reduction and re-formation of the two disulfide bonds cross-linking its single polypeptide chain. The two disulfide bonds of DNase are quantitatively reduced by mercaptoethanol and similar reagents in minutes at pH 7.2 and room temperature, without need for 8 M urea...

kappa-Bungarotoxin, a kappa-neurotoxin derived from the venom of the banded Krait, Bungarus multicinctus, is a homodimeric protein composed of subunits of 66 amino acid residues containing five disulfide bonds. kappa-Bungarotoxin is a potent, selective, and slowly reversible antagonist of alpha3 beta2 neuronal nicotinic acetylcholine receptors. kappa-Bungarotoxin is structurally related to the ...

Most seed storage proteins of the prolamin class accumulate in the endoplasmic reticulum (ER) as large insoluble polymers termed protein bodies (PBs), through mechanisms that are still poorly understood. We previously showed that a fusion between the Phaseolus vulgaris vacuolar storage protein phaseolin and the N-terminal half of the Zea mays prolamin gamma-zein forms ER-located PBs. Zeolin has...