Thioglycolic acid corresponding disulfide (2-[(carboxymethyl)disulfanyl]acetic acid or dithiodiglycolic acid): Thioglycolic acid, usually as its dianion, forms complexes with metal ions. Such complexes have been used for the detection of iron, molybdenum, silver, and tin. Thioglycolic acid reacts with diethyl acetylmalonate to form acetylmercaptoacetic acid and diethyl malonate, the reducing agent in conversion of Fe(III) to Fe(II). Scientist David R. Goddard, in the early 1930s, identified TGA as a useful reagent for reducing the disulfide bonds in proteins, including keratin (hair protein), while studying why protease enzymes could not easily digest hair, nails, feathers, and such. He realized that while the disulfide bonds,
HspQ protein domain could occurs through binding of YccV itself to fully or hemimethylated DNA. In addition, studies have identified the "yccV" gene as one of three insertion sites in mini-Tn10 which suppress dnaA46 thermosensitivity. This protein domain is thought to have a SH3-like barrel structure. Additionally, the structure of a hypothetical protein in this family has been solved and it forms a beta sheet structure with a terminating alpha helix. HspQ forms a stable homodimer in solution and can form homomultimers consisting of about four monomers. The theoretical molecular mass of the HspQ protein were calculated to be 11.8 kDa. It is