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A disulfide bond (SS-bond), also called a disulfide bridge, is a strong covalent bond between two sulfhydryl (-SH) groups. This bond is very important to the folding, structure, and function of proteins.
When two amino acids covalently bond to each other through their side chains, they normally do so through a disulfide bond. The particular side chain involved is the sulfhydryl group (-SH). Oxidation of the thiol group yields a disulfide (S-S) bond. The presence of S-S then helps to maintain the tertiary structure of the protein. An amino acid that commonly forms S-S bonds in proteins is cysteine. When two cysteines are bonded by an S-S bond, the resulting molecule between the two protein chains is called cystine. The figure below shows the formation of a disulfide bond. The R on each side group represents the remainder of the amino acid.
In proteins that contain more than one disulfide bond, proper pairing of the cysteine residues is important for normal structure and activity.
In prokaryotes
Disulfide bonds play an important protective role for bacteria as a reversible switch that turns a protein on or off when bacterial cells are exposed to oxidation reactions. Hydrogen peroxide (H2O2) in particular could severely damage DNA and kill the bacterium at low concentrations if it weren't for the protective action of the SS-bond.
In rubber
Disulfide bonds also play a significant role in the vulcanization of rubber.
In eukaryotes
In eukaryotic cells, disulfide bonds are generally formed in the lumen of the RER (rough endoplasmic reticulum) but not in the cytosol. This is due to the oxidative environment of the ER and the reducing environment of the cytosol (see glutathione). Thus disulfide bonds are mostly found in secretory proteins, lysosomal proteins, and the exoplasmic domains of membrane proteins.
There are notable exceptions to this rule. A number of cytosolic proteins have cysteine residues in proximity to each other that function as oxidation sensors; when the reductive potential of the cell fails, they oxidize and trigger cellular response mechanisms. Vaccinia virus also produces cytosolic proteins and peptides that have many disulfide bonds; although the reason for this is unknown presumably they have protective effects against intracellular proteolysis machinery.
Disulfide bonds are also formed within and between protamines in the sperm chromatin of many mammalian species.
In hair
Hair is a biological polymer, with over 90% of its dry weight made of proteins called keratins. Under normal conditions, human hair contains around 10% water, which modifies its mechanical properties considerably. Hair proteins are held together by disulfide bonds, from the amino acid cysteine. These links are very robust: for example, virtually intact hair has been recovered from ancient Egyptian tombs. Different parts of the hair have different cysteine levels, leading to harder or softer material. Breaking and making disulfide bonds governs the phenomenon of wavy or frizzy hair. It is breaking and remaking of the disulfide bonds which is the basis for the permanent wave.
External links
- Disulfide bonds and hair
- Protein disulfide bond formation in prokaryotes
- Oxidative protein folding in eukaryotes : mechanisms and consequences
- The human protein disulfide isomerase family: substrate interactions and functional properties
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"Disulfide bond"