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,
HHV capsid portal protein HHV capsid portal protein HHV Capsid Portal Protein, or HSV-1 U-6 protein, is the protein which forms a cylindrical portal in the capsid of Herpes simplex virus (HSV-1). The protein is commonly referred to as the "HSV-1 U-6" protein because it is the transcription product of Herpes gene U-6. The Herpes viral DNA enters and exits the capsid via the capsid portal. The capsid portal is formed by twelve copies of portal protein arranged as a ring; the proteins contain a leucine zipper sequence of amino acids which allow them to adhere to each other. Each icosahedral capsid contains a