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,
Protein design protein design programs vary greatly, they have to address four main modeling questions: What is the target structure of the design, what flexibility is allowed on the target structure, which sequences are included in the search, and which force field will be used to score sequences and structures. Protein function is heavily dependent on protein structure, and rational protein design uses this relationship to design function by designing proteins that have a target structure or fold. Thus, by definition, in rational protein design the target structure or ensemble of structures must be known beforehand. This contrasts with other forms of