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Iodoacetamide (IAA) is an organic compound with the chemical formula I C H 2 CO NH 2. It is an alkylating agent used for peptide mapping purposes. Its actions are similar to those of iodoacetate. It is commonly used to bind covalently with the thiol group of cysteine so the protein cannot form disulfide bonds.
It is often used to modify −SH groups to prevent the re-formation of disulfide bonds after the reduction of cystine residues to cysteine during protein sequencing. In 1929, Dr. Einar Lundsgaard (1899-1968) discovered that muscle poisoned in vitro with iodoacetic acid is unable to produce lactate as glycolysis from muscle glycogen is blocked ...
The intervening region (IVR) domain contains two critical cysteine residues, Cys273 and Cys288, which are a second group of cysteines important for stress sensing. A double glycine repeat (DGR) and C-terminal region domains collaborate to form a β-propeller structure, which is where Keap1 interacts with Nrf2 .
N-Ethylmaleimide was used by Arthur Kornberg and colleagues to knock out DNA polymerase III in order to compare its activity to that of DNA polymerase I (pol III and I, respectively). Kornberg had been awarded the Nobel Prize for discovering pol I, then believed to be the mechanism of bacterial DNA replication , although in this experiment he ...
The formation of disulfide bonds from cysteine residues may also be referred to as a post-translational modification. [3] For instance, the peptide hormone insulin is cut twice after disulfide bonds are formed, and a propeptide is removed from the middle of the chain; the resulting protein consists of two polypeptide chains connected by ...
The site-directed covalent warhead, also called a covalent modifier, is an electrophile that covalently modifies a serine, cysteine, or lysine residue in the enzyme's active site and prevents future interactions with other ligands. [7]
Initial treatment is with adequate hydration, alkalization of the urine with citrate supplementation or acetazolamide, and dietary modification to reduce salt and protein intake (especially methionine). If this fails then patients are usually started on chelation therapy with an agent such as penicillamine. [8] [9] Tiopronin is another agent ...
Phosphorylation occurs when a PO 3 (phosphoryl) group is added to a protein. [3] This chemical modification is the most extensively studied and is reversible. The result of those studies has shown that phosphorylation acts as a regulator for proteins in two ways: the addition or removal of phosphoryl group can impact enzyme kinetics by turning on or off the enzymatic function via ...