A disulfide is a compound containing an -S-S- linkage. (Organic) sulfides have the structure R-S-R′, and are therefore the sulfur analogues of ethers. The nomenclature of sulfides can be easily understood if one understands the nomenclature of the corresponding ethers. Notice that the term “thio” is also used in inorganic chemistry The formation of disulfide bonds (DSBs) in proteins is an oxidative process that generates a covalent bond linking the sulfur atoms of two cysteine residues. DSBs Disulfide bonds form covalent bonds between distal regions of peptides and proteins to dramatically impact their folding, stability, and oligomerization. Given the prevalence of disulfide bonds in many natural products, considerable effort has been invested in site-selective disulfide bond formation approaches to control the folding of Our results identify cysteines 10as a redox-sensitive pair that forms an intersubunit disulfide bond between neighboring RyR2 subunits during Addition of the reducing agent dithiothreitol (DTT) to the medium of living cells prevented disulfide bond formation in newly synthesized influenza hemagglutinin Disulfide, as a common structural motif, has been frequently used in pharmaceuticals, nature products, and chemical biology. This chapter focuses on the methodologies that were reported recently for the synthesis of disulfide-containing compounds with particular emphasis on the synthesis of unsymmetrical disulfides. The
Disulfide formation in the ER and mitochondria: two solutions to …
Disulfide-Bond-Forming Pathways in Gram-Positive Bacteria. Melissa E. Reardon-Robinson and Hung Ton-That. W. Margolin, Editor. Author information Mechanisms of disulfide bond formation in the human pathogen Streptococcus pyogenes are currently unknown. To date, no disulfide bond-forming thiol-disulfide oxidoreductase (TDOR) has been described and at least one disulfide bonded protein is known in S. [HOST] protein is the superantigen SpeA, which contains 3 cysteine residues A method to mimic the complex chemistry of disulfide bond formation in molecular simulations is developed, which is used to decipher the mechanism of folding of bovine pancreatic trypsin inhibitor and establishes that it is the conformational folding of the protein that directs disulfite bond formation. PDF The Formation of Native Disulfide Bonds: Treading a Fine Line in Protein Folding. Published: 25 March Volume 40, pages –, () Cite this
Identification of in Vivo Disulfide Conformation of TRPA1 Ion Channel ...
Abstract Significance: The discovery of the oxidoreductase disulfide bond protein A (DsbA) in opened the way to the unraveling of the pathways of disulfide bond formation in the periplasm of Escherichia coli and other Gram-negative bacteria. Correct oxidative protein folding in the E. coli envelope depends on both the DsbA/DsbB Delayed oxygen-independent disulfide bond formation after translation in DTT. HeLa cells transfected with LDLR (A and B), VEGF-A (C and D), or CA9 (E and F) were 35 S pulse labeled in the presence of 5 mM DTT for 15 min under the indicated % O 2. Proteins were subsequently allowed to fold in DTT-free media for the indicated chase The CXXC active-site motif of PDI is also found in homologous thiol–disulfide oxidoreductases [7].In bacteria, the pathway for native disulfide bond formation involves the CXXC-containing Dsb family of proteins (DsbA–D) and may be analogous to the eukaryotic pathway [8].This review will focus on intriguing new insights into the Based on this thermodynamic model, the relative rates of protein folding and disulfide bond formation for nascent peptides have important consequences for oxidative stress (Figure 4b). When folding is faster than disulfide bond formation, ROS is produced in near one-to-one amounts with the disulfide bonds formed