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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... |
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... |
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... |
disruption of: Covalent interactions between amino acid side-chains (such as disulfide bridges between cysteine groups) Non-covalent dipole-dipole interactions... |
protecting groups used in peptide synthesis requiring later regioselective disulfide bond formation must possess multiple characteristics. First, they must be... |
quenching of its fluorescence. However, upon breakage of disulfide bond by protein disulfide-isomerase, fluorescence increases 70-fold. Redox dysregulation... |
Covalent radius Disulfide bond Hybridization Hydrogen bond Ionic bond Linear combination of atomic orbitals Metallic bonding Noncovalent bonding Resonance (chemistry)... |
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... |
DsbA (redirect from Disulfide bond formation protein A) 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... |
Thiol (section Structure and bonding) 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... |
Glutathione reductase (redirect from Glutathione-disulfide 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... |
Conotoxin (section Disulfide connectivities) 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... |
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... |
Thioredoxin reductase (redirect from Thioredoxin-disulfide reductase) 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:... |
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... |