Disulphide bridges: Difference between revisions
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A disulphide bridge can also be called a disulphide bond. It is the name of the [[Covalent bond]] that is formed when two thiol groups, SH groups, undergo [[Oxidation]] and a bond forms between the two Sulphur atoms. In the formation of this type of bond, two [[Protons]] and two [[Electron]]s are produced as biproducts. | A disulphide bridge can also be called a [[Disulphide bond|disulphide bond]]. It is the name of the [[Covalent bond|covalent bond]] that is formed when two thiol groups, SH groups, undergo [[Oxidation|oxidation]] and a bond forms between the two [[Sulphur|sulphur]] atoms. In the formation of this type of bond, two [[Protons|protons]] and two [[Electron|electron]]s are produced as biproducts. | ||
Disulphide bonds are often present in [[Tertiary Protein Structure]] between [[Cysteine]] residues, as they help to stabilise the protein. The S-S bonds are formed as part of the folding of the protein into its final 3D structure in the [[Endoplasmic reticulum]]<ref>http://www.ncbi.nlm.nih.gov/pubmed/10754564</ref>. | Disulphide bonds are often present in [[Tertiary Protein Structure|tertiary protein structure]] between [[Cysteine|cysteine]] residues, as they help to stabilise the protein. The S-S bonds are formed as part of the folding of the protein into its final 3D structure in the [[Endoplasmic reticulum]]<ref>http://www.ncbi.nlm.nih.gov/pubmed/10754564</ref>. | ||
The disulphide bonds only occur on the extracellular domains of a protein, as in the [[Cytosol]] (a reducing environment) the bonds become unstable and break. | The disulphide bonds only occur on the extracellular domains of a protein, as in the [[Cytosol]] (a reducing environment) the bonds become unstable and break. | ||
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= References = | = References = | ||
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Revision as of 20:25, 17 November 2010
A disulphide bridge can also be called a disulphide bond. It is the name of the covalent bond that is formed when two thiol groups, SH groups, undergo oxidation and a bond forms between the two sulphur atoms. In the formation of this type of bond, two protons and two electrons are produced as biproducts.
Disulphide bonds are often present in tertiary protein structure between cysteine residues, as they help to stabilise the protein. The S-S bonds are formed as part of the folding of the protein into its final 3D structure in the Endoplasmic reticulum[1].
The disulphide bonds only occur on the extracellular domains of a protein, as in the Cytosol (a reducing environment) the bonds become unstable and break.