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...

quenching of its fluorescence. However, upon breakage of disulfide bond by protein disulfide-isomerase, fluorescence increases 70-fold. Redox dysregulation...

protecting groups used in peptide synthesis requiring later regioselective disulfide bond formation must possess multiple characteristics. First, they must be...

increases the top-down MS sequence coverage of disulfide bond containing proteins and cleaves a disulfide bond homolytically to produce two separated thiol...

Covalent radius Disulfide bond Hybridization Hydrogen bond Ionic bond Linear combination of atomic orbitals Metallic bonding Noncovalent bonding Resonance (chemistry)...

folding. For example, disulfide bond protein A (DsbA) and disulfide bond protein C (DsbC), which are responsible for catalyzing peptide bond formation and isomerization...

membrane, and is essential for the oxidation of protein dithiols. Since disulfide bond formation is an oxidative process, the major pathway of its catalysis...