Disulfide bridges in proteins are made of covalent bonds between two sulfurs adjacent to each other in a protein. Therefore Cysteines who's side groups have sulfurs are significant determining the position and number of S=S bonds in a protein. Because covalent bonds are the strongest bonds, they stabilize a protein making it is hard to denature. The more the S=S bonds the higher the stability of the protein. An example of proteins with S=S bonds is keratin, the protein that makes nails and curly hair.
The change leads to increased protein stability because of an increased number of S-S bonds in the tertiary structure of protein.
Explanation:
Disulfide bond:
This is the bond in which sulfur of one amino acid forms a covalent bond with the sulfur of another amino acid.
Proteins contain normally two amino acids which have sulfur in their structure these are Methionine and cysteine
Disulfide bridges formation:
The disulfide bridges are formed by the oxidation of cysteine with the sulfhydryl groups. These bridges are important in the stabilization of the protein tertiary structure. These disulfide bridges are also responsible for bringing the hydrogen bonds closer in two parts of a chain.
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The change leads to increased protein stability because of an increased number of S-S bonds in the tertiary structure of a protein.
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