Disulfide bond

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  • group or the S2− 2 anion. The linkage is also called an SS-bond or sometimes a disulfide bridge and usually derived from two thiol groups. In inorganic...
  • Thumbnail for Immunoglobulin M
    both by disulfide bonds (depicted as red triangles) and by non-covalent interactions. Figure 1B shows two µL units linked by a disulfide bond in the Cµ2...
  • Thumbnail for Dithiothreitol
    internal disulfide bond. It has a redox potential of −0.33 V at pH 7. The reduction of a typical disulfide bond proceeds by two sequential thiol-disulfide exchange...
  • Thumbnail for Denaturation (biochemistry)
    disruption of: Covalent interactions between amino acid side-chains (such as disulfide bridges between cysteine groups) Non-covalent dipole-dipole interactions...
  • Thumbnail for Peptide synthesis
    protecting groups used in peptide synthesis requiring later regioselective disulfide bond formation must possess multiple characteristics. First, they must be...
  • Thumbnail for Protein disulfide-isomerase
    quenching of its fluorescence. However, upon breakage of disulfide bond by protein disulfide-isomerase, fluorescence increases 70-fold. Redox dysregulation...
  • Thumbnail for Covalent bond
    Covalent radius Disulfide bond Hybridization Hydrogen bond Ionic bond Linear combination of atomic orbitals Metallic bonding Noncovalent bonding Resonance (chemistry)...
  • Thumbnail for Electron-capture dissociation
    increases the top-down MS sequence coverage of disulfide bond containing proteins and cleaves a disulfide bond homolytically to produce two separated thiol...
  • folding. For example, disulfide bond protein A (DsbA) and disulfide bond protein C (DsbC), which are responsible for catalyzing peptide bond formation and isomerization...
  • Thumbnail for DsbA
    thiol disulfide oxidoreductase (TDOR). DsbA is a key component of the Dsb (disulfide bond) family of enzymes. DsbA catalyzes intrachain disulfide bond formation...
  • Sulfide (section Disulfides)
    carbon disulfide has no S–S bond, being S=C=S (linear molecule analog to CO2). Most often in sulfur chemistry and in biochemistry, the disulfide term is...
  • Thumbnail for Thiol
    an oxidation reaction can generate a cystine unit with a disulfide bond (−S−S−). Disulfide bonds can contribute to a protein's tertiary structure if...
  • Thumbnail for Glutathione reductase
    anion. This anion then quickly breaks a disulfide bond of Cys58 - Cys63, forming a short lived covalent bond a stable charge-transfer complex between...
  • Thumbnail for Conotoxin
    very special disulfide-through-disulfide knot, in which the III-VI disulfide bond crosses the macrocycle formed by two other disulfide bonds (I-IV and...
  • Thumbnail for Ricin
    functionally equivalent to a type 1 RIP, covalently connected by a single disulfide bond to a B chain that is catalytically inactive, but serves to mediate transport...
  • NADPH binding domain, and an active site containing a redox-active disulfide bond. Thioredoxin reductases are enzymes that catalyze the reduction of thioredoxin...
  • alpha-chymotrypsin, which has three polypeptide chains linked by two of the five disulfide bond present in the primary structure of chymotrypsinogen. Examples of zymogens:...
  • Thumbnail for Three-finger toxin
    have under 66 residues and four core disulfide bonds. long-chain toxins have at least 66 residues, a disulfide bond in loop II, and possibly a C-terminal...
  • low-molecular-mass subunits held together by disulfide bonds.[citation needed] The way the glutenins form their disulfide bond network is predicted to be regulated...
  • Kell blood group antigen. The Kell glycoprotein links via a single disulfide bond to the XK membrane protein that carries the Kx antigen. The encoded...
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