Disulfide Bonds


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Disulfide Bonds

 

(—S—S— bonds), bonds that are formed by the union of sulfur atoms of two mercapto groups. Crosslinking of polypeptide chains containing residues of the amino acid cysteine takes place with the formation of disulfide bonds.

References in periodicals archive ?
Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm.
P-5125; Sigma) at 37[degrees]C for 1 h, a treatment that cleaves disulfide bonds in the IgM pentamer through the thiol activity of penicillamine.
High pressure processing of the milk used to make cheese causes a denaturation of whey proteins that form disulfide bonds with casein micelles.
By breaking the disulfide bonds that help form the shape of HIV's surface, he suggests, PDI allows the virus to fuse with the cell membrane.
Curling hair permanently would not be possible without breaking these disulfide bonds. This is accomplished by treating the hair with alkaline reducing agents such as ammonium thioglycolate in an ammoniac solution (pH of about 9.5).
One of the most critical steps in the sample-processing procedure is the reduction of disulfide bonds before derivatization (14).
Whey protein forms an intact water-insoluble film out of aqueous solution, due to the formation of intermolecular disulfide bonds after heat denaturation.
Cysteine may form disulfide bonds, which in turn can form strong links between protein molecules, microbiologist Frances D.
Specifically, Escalol[R] HP protects the hair from UV-B radiation that can cleave disulfide bonds, decompose tryptophan, roughen hair (a key consumer perceivable signal), and lead to hair breakage.
The poor stability of GSH, well documented for HPLC analysis, could be prevented by addition of NEM or potassium borohydride to trap thiols or reduce disulfide bonds (1, 7).
As disulfide bonds photodegrade, hair experiences a loss in cystine content and a corresponding increase in cysteic acid.
(a) Serum disulfide bonds are reduced to release Hcy as monothiol;