Disulfide bond

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Disulfide Bond

A Disulfide Bond (pronunciation: /daɪˈsʌlfaɪd bɒnd/), also known as a Sulfur Bridge, is a covalent bond derived from two thiol groups.

Etymology

The term "Disulfide Bond" originates from the prefix 'di-' meaning 'two' in Greek, and 'sulfide' which is derived from the Latin 'sulfur' meaning 'brimstone'.

Definition

A Disulfide Bond is a single covalent bond formed through the oxidation of two thiol groups. The overall process is a redox reaction, in which two thiolate anions are coupled to form a disulfide bond and release two electrons.

Function

Disulfide bonds play a crucial role in the folding and stability of some proteins, usually those secreted to the extracellular medium. The bond is a post-translational modification and is formed by the enzyme protein disulfide isomerase (PDI). It is one of the most common types of stable covalent bonds that form between proteins in cells.

Related Terms

  • Thiol: An organic compound containing a sulfur and a hydrogen atom.
  • Redox: A type of chemical reaction that involves a transfer of electrons between two species.
  • Protein: Large biomolecules and macromolecules that are composed of one or more long chains of amino acid residues.
  • Protein Disulfide Isomerase (PDI): An enzyme in the endoplasmic reticulum in eukaryotes and the periplasm of bacteria that catalyzes the formation and breakage of disulfide bonds between cysteine residues within proteins as they fold.

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