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,
Ribosomal protein leader form an intrinsic transcription termination stem-loop. When cellular concentrations of the ribosomal protein are not high, they are occupied in the ribosome, and are not available in significant quantities to bind the mRNA leader. This leads to increased expression of the gene, which leads to the synthesis of more copies of the ribosomal protein. Many examples of ribosomal protein leaders are known in bacteria, including ribosomal protein L20 leader and ribosomal S15 leader. Ribosomal protein leader A ribosomal protein leader is a mechanism used in cells to control the cellular concentration of a protein that forms a part of the