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A disulfide ensemble is a grouping of all disulfide species with the same number of disulfide bonds, and is usually denoted as the 1S ensemble, the 2S ensemble, etc. for disulfide species having one, two, etc. disulfide bonds. Thus, the (26–84) disulfide species belongs to the 1S ensemble, whereas the (26–84, 58–110) species belongs to ...
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]
TCEP is often used as a reducing agent to break disulfide bonds within and between proteins as a preparatory step for gel electrophoresis.. Compared to the other two most common agents used for this purpose (dithiothreitol and β-mercaptoethanol), TCEP has the advantages of being odorless, a more powerful reducing agent, an irreversible reducing agent (in the sense that TCEP does not ...
By transferring the disulfide bond between these two cysteine residues onto the folding protein it is responsible for the latter's oxidation. In contrast to bacteria, where the oxidative and isomerization pathways are carried out by different proteins, PDI is also responsible for the reduction and isomerization of the disulfide bonds.
It is commonly used to bind covalently with the thiol group of cysteine so the protein cannot form disulfide bonds. [ 2 ] [ 3 ] It is also used in ubiquitin studies as an inhibitor of deubiquitinase enzymes (DUBs) because it alkylates the cysteine residues at the DUB active site.
The formation of multiple native disulfides remains challenging of native peptide synthesis by solid-phase methods. Random chain combination typically results in several products with nonnative disulfide bonds. [41] Stepwise formation of disulfide bonds is typically the preferred method, and performed with thiol protecting groups. [42]
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.
The primary function of thioredoxin (Trx) is the reduction of oxidized cysteine residues and the cleavage of disulfide bonds. [10] Multiple in vitro substrates for thioredoxin have been identified, including ribonuclease, choriogonadotropins, coagulation factors, glucocorticoid receptor, and insulin.