Results (
Thai) 1:
[Copy]Copied!
3.1.5.1 Disulfide Bonds Two cysteine residues can cross-link, through an oxidative process, to form a sulfur—sulfur bond, referred to as a disulfide bond. These cross links can occur intramolecularly, between two cysteines within a single polypeptide, or intermolecularly, to join two polypeptides together. Such disulfide bond cross-linking can provide stabilizing energy to the folded conformation of the protein. Numerous examples exist of proteins that utilize both inter- and intramolecular disulfide bonds in their folded forms. Intermolecular disulfide bonds can also occur between a cysteine residue on aprotein and a sulfhydryl group on a small molecule ligand or modifying reagent. For example, 4,4-dithioldipyridine is a reagent used to quantify the number of free cysteines (those not involved in disulfide bonds) in proteins. The reagent reacts with the free sulfhydryls to form intermolecular disulfide bonds, with the liberation of a chromophoric by-product. The formation of the by-product is stoichiometric with reactive cysteines. Thus, one can quantify the number of cysteines that reacted from the absorbance of the by-product.
Being translated, please wait..