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The structure of a disulfide bond can be described by its χ ss dihedral angle between the C β −S γ −S γ −C β atoms, which is usually close to ±90°. The disulfide bond stabilizes the folded form of a protein in several ways: It holds two portions of the protein together, biasing the protein towards the folded topology.
Conversion of simple disulfides to thiosulfinates results in a considerable weakening of the S–S bond from about 47.8 to 28.0 kcal mol −1 for the S-S bond in PhS(O)SPh and from about 63.2 to 39.3 kcal mol −1 for the S-S bond in MeS(O)SMe, [14] with the consequence that most thiosulfinates are both unstable and quite reactive.
DsbC (Disulfide bond C) is a prokaryotic disulfide bond isomerase. The formation of native disulfide bonds play an important role in the proper folding of proteins and stabilize tertiary structures of the protein. [1] [2] [3] DsbC is one of 6 proteins in the Dsb family in prokaryotes. The other proteins are DsbA, DsbB, DsbD, DsbE and DsbG. [4]
The structure of hydrogen disulfide is similar to that of hydrogen peroxide, with C 2 point group symmetry. Both molecules are distinctly nonplanar. The dihedral angle between the H a −S−S and S−S−H b planes is 90.6°, compared with 111.5° in H 2 O 2. The H−S−S bond angle is 92°, close to 90° for unhybridized divalent sulfur. [1]
Cysteine (/ ˈ s ɪ s t ɪ iː n /; [5] symbol Cys or C [6]) is a semiessential [7] proteinogenic amino acid with the formula HOOC−CH(−NH 2)−CH 2 −SH. The thiol side chain in cysteine enables the formation of disulfide bonds, and often participates in enzymatic reactions as a nucleophile. Cysteine is chiral, but both D and L-cysteine ...
DsbA is a bacterial thiol disulfide oxidoreductase (TDOR). DsbA is a key component of the Dsb (disulfide bond) family of enzymes. DsbA catalyzes intrachain disulfide bond formation as peptides emerge into the cell's periplasm. [2] Structurally, DsbA contains a thioredoxin domain with an inserted helical domain of unknown function. [3]
Chemical formula. C 10 H 8 N 2 S 2: Molar mass: ... It is also used in molecular biology as an oxidising agent, for example to oxidise free thiols to form disulfide ...
The free sulfhydryls of fibronectin are not required for the binding of fibronectin to the cell layer or for its subsequent incorporation into the extracellular matrix. Disulfide-bonded multimerization of fibronectin in the cell layer occurs by disulfide bond exchange in the disulfide-rich amino-terminal one-third of the molecule. [32]