A strong covalent bond between two sulfur atoms.
A covalent linkage between two cysteine residues in different parts of a protein or between two different proteins. Insulin (a small protein having two polypeptide chains) and immunoglobulin molecules, for example, have interchain and intrachain disulfide bonds. HLA molecules also have disulfide bonds. The C282Y mutation removes one of the disulfide bonds in the HLA class I-like HFE protein and abolishes its surface expression.
A covalent bond created between sulfur atoms in two molecules of the amino acid cysteine, located at different points in the amino acid chain of a folding protein or peptide. The disulfide bond is often necessary for a protein to fold correctly and be fully functional.
a bond between two sulfur atoms, protein-SS-protein,
a covalent bond between the sulfur atoms in two cyst e ine residues (reduced form), forming one cystine (one oxidized cyst e ine dimer)
A covalent bond formed between two sulfur atoms of different cysteines in a protein.
A chemical bond that contains two sulfur atoms.
a bond between two sulfur atoms. In the context of a protein molecule, this type of bond often forms between two sulfur atoms contained in cysteine molecules located in the amino acid sequence that makes up the protein.
a sulfur to sulfur bond found in both normal and abnormal cross-linked proteins, bonding a protein to parts of the same molecule of to other molecules. These bonds provide the three dimensional structure of molecule containing them. Latex is vulcanized to form rubber by the controlled formation of disulfide bonds.
A common covalent linkage between the sulfhydryl groups on two cysteine residues in different proteins or in different parts of the same protein; generally found only in extracellular proteins or protein domains.
In chemistry, a disulfide bond is a single covalent bond derived from the coupling of thiol groups. The linkage is also called an SS-bond or disulfide bridge. The overall connectivity is therefore C-S-S-C.