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  • hydrogen peroxide
  • Diallyl disulfide can be readily oxidized to allicin with hydrogen peroxide or peracetic acid. (wikipedia.org)
  • Typical oxidants are chlorine and hydrogen peroxide: 2 R2NCSSNa + Cl2 → (R2NCSS)2 + 2 NaCl Thiuram disulfides react with Grignard reagents to give esters of dithiocarbamic acid, as in the preparation of methyl dimethyldithiocarbamate: [Me2NC(S)S]2 + MeMgX → Me2NC(S)SMe + Me2NCS2MgX The compounds feature planar dithiocarbamate subunits and are linked by an S−S bond of 2.00 Å. (wikipedia.org)
  • The structure of hydrogen disulfide is similar to that of hydrogen peroxide, with C2 point group symmetry. (wikipedia.org)
  • dithiol
  • This dithiol pair attacks the periplasmic N-terminal disulfide bridge at C103 and C109 (C1 and C2, respectively) which transfers electrons to DsbC and other protein electron acceptors as noted above. (wikipedia.org)
  • Molecular
  • in contrast, the high-molecular-weight glutenins are formed by disulfide linkages of several diverse polypeptide chains which have been separated and characterized. (springer.com)
  • hydrogenation
  • Although the hydrogenation of disulfides is usually not practical, the equilibrium constant for the reaction provides a measure of the standard redox potential for disulfides: RSSR + H2 → 2 RSH This value is about −250 mV versus the standard hydrogen electrode (pH = 7). (wikipedia.org)
  • reaction
  • The overall vectorial electron transfer reaction catalyzed by DsbD is: 2 e− cytoplasm → 2 e− periplasm DsbB contains 4 essential cysteine residues, reversibly forming two disulfide bonds. (wikipedia.org)
  • protein
  • The prototype of a protein disulfide bond is the two-amino-acid peptide, cystine , which is composed of two cysteine amino acids joined by a disulfide bond (shown in Figure 2 in its unionized form). (wikidoc.org)
  • The disulfide bond stabilizes the folded form of a protein in several ways: 1) It holds two portions of the protein together, biasing the protein towards the folded topology. (wikidoc.org)
  • Expressed differently, the disulfide bond destabilizes the unfolded form of the protein by lowering its entropy . (wikidoc.org)
  • 2) The disulfide bond may form the nucleus of a hydrophobic core of the folded protein, i.e., local hydrophobic residues may condense around the disulfide bond and onto each other through hydrophobic interactions . (wikidoc.org)
  • 3) Related to #1 and #2, the disulfide bond link two segments of the protein chain, the disulfide bond increases the effective local concentration of protein residues and lowers the effective local concentration of water molecules. (wikidoc.org)
  • Protein disulfide-isomerase has two catalytic thioredoxin-like domains (active sites), each containing the canonical CGHC motif, and two non catalytic domains. (wikipedia.org)
  • PDI displays oxidoreductase and isomerase properties, both of which depend on the type of substrate that binds to protein disulfide-isomerase and changes in protein disulfide-isomerase's redox state. (wikipedia.org)
  • a second cysteine residue binds to the complex, whereby after subsequent catalysis, a stable disulfide bridge on the substrate is formed, leaving protein disulfide-isomerase's cysteine residues reduced. (wikipedia.org)
  • Therefore, protein disulfide-isomerase is capable of catalyzing the post-translational modification disulfide exchange. (wikipedia.org)
  • In the chloroplasts of the unicellular algae Chlamydomonas reinhardtii the protein disulfide-isomerase RB60 serves as a redox sensor component of an mRNA-binding protein complex implicated in the photoregulation of the translation of psbA, the RNA encoding for the photosystem II core protein D1. (wikipedia.org)
  • Protein disulfide-isomerase has also been suggested to play a role in the formation of regulatory disulfide bonds in chloroplasts. (wikipedia.org)
  • Protein disulfide-isomerase helps load antigenic peptides into MHC class I molecules. (wikipedia.org)
  • Protein disulfide-isomerase has been found to be involved in the breaking of bonds on the HIV gp120 protein during HIV infection of CD4 positive cells, and is required for HIV infection of lymphocytes and monocytes. (wikipedia.org)
  • thiol
  • In chemistry , a disulfide bond is a single covalent bond derived from the coupling of thiol groups. (wikidoc.org)
  • In chemistry, a disulfide refers to a functional group with the structure R−S−S−R′. The linkage is also called an SS-bond or sometimes a disulfide bridge and is usually derived by the coupling of two thiol groups. (wikipedia.org)
  • Hence, thiol-disulfide exchange is inhibited at low pH (typically, below 8) where the protonated thiol form is favored relative to the deprotonated thiolate form. (wikipedia.org)
  • redox
  • Oxidoreductase Redox Disulfide DsbA Transporter Classification Database TCDB: 5.A.1 The Disufide Bond Oxidoreductase D (DsbD) Family Bardischewsky, F. (wikipedia.org)
  • alkali
  • Intercalation can be conducted by combining a suspension of the disulfide material and a solution of the alkali metal in anhydrous ammonia. (wikipedia.org)
  • hexane
  • therefore, diallyl disulfide is insoluble in water and is soluble in fats, oils, lipids, and non-polar solvents such as hexane or toluene. (wikipedia.org)
  • Thus
  • Thus, Alliaceae plants have likely developed the diallyl disulfide-TRPA1 protection mechanism against predators at the early stages of the evolution. (wikipedia.org)
  • bond
  • The linkage is also called an SS-bond or disulfide bridge. (wikidoc.org)
  • A disulfide bond is typically denoted by hyphenating the abbreviations for cysteine, e.g., the "Cys26-Cys84 disulfide bond", or the "26-84 disulfide bond", or most simply as "C26-C84" where the disulfide bond is understood and does not need to be mentioned. (wikidoc.org)
  • Since water molecules attack amide-amide hydrogen bonds and break up secondary structure , a disulfide bond stabilizes secondary structure in its vicinity. (wikidoc.org)
  • For example, researchers have identified several pairs of peptides that are unstructured in isolation, but adopt stable secondary and tertiary structure upon forming a disulfide bond between them. (wikidoc.org)
  • The disulfide bonds are strong, with a typical bond dissociation energy of 60 kcal/mol (251 kJ mol−1). (wikipedia.org)
  • However, being about 40% weaker than C−C and C−H bonds, the disulfide bond is often the "weak link" in many molecules. (wikipedia.org)