disulfide bond


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bond

 [bond]
the linkage between atoms or radicals of a chemical compound, or the symbol representing this linkage and indicating the number and attachment of the valencies of an atom in constitutional formulas, represented by a pair of dots or a line between atoms, e.g., H—O—H, H—C≡C—H or H:O:H, H:C:::C:H.
coordinate covalent bond a covalent bond in which one of the bonded atoms furnishes both of the shared electrons.
covalent bond a chemical bond between two atoms or radicals formed by the sharing of a pair (single bond), two pairs (double bond), or three pairs of electrons (triple bond).
disulfide bond a strong covalent bond, —S—S—, important in linking polypeptide chains in proteins, the linkage arising as a result of the oxidation of the sulfhydryl (SH) groups of two molecules of cysteine.
high-energy phosphate bond an energy-rich phosphate linkage present in adenosine triphosphate (ATP), phosphocreatine, and certain other biological molecules. On hydrolysis at pH 7 it yields about 8000 calories per mole, in contrast to the 3000 calories yielded by phosphate esters. The bond stores energy that is used to drive biochemical processes, such as the synthesis of macromolecules, contraction of muscles, and the production of the electrical potentials for nerve conduction.
high-energy sulfur bond an energy-rich sulfur linkage, the most important of which occurs in the acetyl-CoA molecule, the main source of energy in fatty acid biosynthesis.
hydrogen bond a weak, primarily electrostatic, bond between a hydrogen atom bound to a highly electronegative element (such as oxygen or nitrogen) in a given molecule, or part of a molecule, and a second highly electronegative atom in another molecule or in a different part of the same molecule.
ionic bond a chemical bond in which electrons are transferred from one atom to another so that one bears a positive and the other a negative charge, the attraction between these opposite charges forming the bond.
peptide bond the —CO—NH— linkage formed between the carboxyl group of one amino acid and the amino group of another; it is an amide linkage joining amino acids to form peptides.

di·sul·fide bond

a single bond between two sulfurs; specifically, the -S-S- link binding two peptide chains (or different parts of one peptide chain); also occurs as part of the molecule of the amino acid, cystine, and is important as a structural determinant in many peptide and protein molecules, for example, keratin, insulin, and oxytocin. A symmetric disulfide is R-S-S-R; R'-S-S-R is a mixed or asymmetric disulfide.

di·sul·fide bond

(dī-sŭl'fīd bond)
A single bond between two sulfurs; specifically, the -S-S- link binding two peptide chains (or different parts of one peptide chain).
Synonym(s): disulphide bond.

bond

the linkage between atoms or radicals of a chemical compound, or the symbol representing this linkage and indicating the number and attachment of the valencies of an atom in constitutional formulas, e.g. H−O−H, H−C= C−H and can be represented by a pair of dots between atoms, e.g. H:O:H, H:C:::C:H.

coordinate covalent bond
a covalent bond in which one of the bonded atoms furnishes both of the shared electrons.
covalent bond
a chemical bond between two atoms or radicals formed by the sharing of a pair (single bond), two pairs (double bond) or three pairs of electrons (triple bond).
disulfide bond
a strong covalent bond, −S−S−, important in linking polypeptide chains in proteins, the linkage arising as a result of the oxidation of the sulfhydryl (SH) groups of two molecules of cysteine.
high-energy phosphate bond
an energy-rich phosphate linkage present in adenosine triphosphate (ATP), phosphocreatine and certain other biological molecules. On hydrolysis at pH 7 it yields about 8000 calories per mole, in contrast to the 3000 calories yielded by phosphate esters. The bond stores energy that is used to drive biochemical processes, such as the synthesis of macromolecules, contraction of muscles, and the production of the electrical potentials for nerve conduction.
high-energy sulfur bond
an energy-rich sulfur linkage, the most important of which occurs in the acetyl-CoA molecule, the main source of energy in fatty acid biosynthesis.
human-animal bond
the psychological interdependence between humans and companion animals.
hydrogen bond
a weak, primarily electrostatic, bond between a hydrogen atom bound to a highly electronegative element (such as oxygen or nitrogen) in a given molecule, or part of a molecule, and a second highly electronegative atom in another molecule or in a different part of the same molecule.
ionic bond
a chemical bond in which electrons are transferred from one atom to another so that one bears a positive and the other a negative charge, the attraction between these opposite charges forming the bond.
peptide bond
the −CO−NH− linkage formed between the carboxyl group of one amino acid and the amino group of another; it is an amide linkage joining amino acids to form peptides.
phosphoanhydride bond
a high energy bond present in ATP.
phosphodiester bond
links between nucleotides in nucleic acids.
References in periodicals archive ?
Single-chain immunotoxin fusions between anti-Tac and Pseudomonas exotoxin: Relative importance of the two toxin disulfide bonds.
This deleted variant of tPA has lost three structural domains of Kringle I, Finger, and EGF, while retaining the thrombolytic Kringle II and protease domains and contains 9 disulfide bonds.
The rigidity and high glass transition (Tg) characteristics of these epoxy polymers reduce or impede the mobility of the crosslinked network making the metathesis of the disulfide bonds difficult.
In (a), PDI catalyzes reduction of a disulfide bond to a dithiol through an attack from its thiolate anion located in [Cys.
2]S-targeting receptor protein kinase with its novel Cys1045-Cys1024 disulfide bond serving as a specific molecular switch for hydrogen sulfide actions in vascular endothelial cells.
Molecular modeling studies have suggested four of these cysteines form two disulfide bonds necessary for furin function.
Moreover, according to our data, closely located cysteine residues which could form disulfide bond are directed into the cavity containing glutathione.
Inadequate disulfide bond generation: Disulfide bridges stabilize protein structure but can be a challenge to correctly form and maintain.
The C-terminal region contains a ring structure formed by a disulfide bond between the cysteine residues in position 86 and 102 (Fig.
Hinge region design: The possibility of multiple varieties of disulfide bond formation makes it possible to have many hinge linkages and probably some undesired forms of antibody fragment (13).
The cholesterol moiety is incorporated into the membrane and the mistletoe lectin is bound via a disulfide bond to the activated maleimido group at room temperature.
We have attempted to prove that these cysreine residues participate in disulfide bond formation.