Disulfide bridge
Disulfide Bridge
A Disulfide bridge or Disulfide bond is a single covalent bond derived from the coupling of thiol groups in an oxidation reaction. This bond is a post-translational modification that occurs in the protein folding process and plays a crucial role in the stability and function of many proteins.
Overview[edit | edit source]
Disulfide bridges are formed by the oxidation of two cysteine residues, which results in the formation of a cystine molecule. This reaction is catalyzed by the enzyme protein disulfide isomerase (PDI). The formation of a disulfide bridge can result in a significant conformational change in the protein, which can affect its function.
Role in Protein Structure[edit | edit source]
Disulfide bridges play a crucial role in the tertiary structure of proteins. They help to stabilize the protein structure by forming covalent links between parts of the protein molecule that are far apart in the sequence but brought together in the folded structure. This can result in a significant increase in the stability of the protein.
Role in Protein Function[edit | edit source]
In addition to their role in protein structure, disulfide bridges can also play a role in the function of proteins. For example, they can be involved in the formation of active sites in enzymes, or they can play a role in the regulation of protein activity.
Disulfide Bridge in Disease[edit | edit source]
Abnormalities in disulfide bridge formation can lead to a variety of diseases. For example, mutations that affect the formation of disulfide bridges can lead to diseases such as cystic fibrosis and Alzheimer's disease. In addition, the disruption of disulfide bridges can lead to the misfolding of proteins, which can result in diseases such as Parkinson's disease and Huntington's disease.
See Also[edit | edit source]
- Protein structure
- Protein folding
- Oxidation reaction
- Cysteine
- Cystic fibrosis
- Alzheimer's disease
- Parkinson's disease
- Huntington's disease
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Contributors: Prab R. Tumpati, MD
