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 ?
Keratin is a protein that contains disulfide bonds and has an array of characteristics that ranges from a structurally robust, impact-resistant material (horn) to a simple waterproof layer (turtle shell).
A Mucolytic Element: Potassium iodide (P1) is used traditionally as a mucolytic, because of its ability to break up disulfide bonds.
These observations and the fact that biosynthetic processing in the liver hepatocyte requires noncovalent association prior to disulfide bond formation indicates C8[alpha] and C8[gamma] contain mutually recognizable binding sites.
DISULFIND server shows that the position of six cysteine peptides of gambicin could not favour disulfide bond formation and shows less stable structure.
The formation of cysteine-homocysteine disulfides has been suggested to disrupt the intramolecular disulfide bonds in fibrillin-1 (7).
These proteins required extensive N-glycosylation and disulfide bonds to maintain their antigencity.
There are already disulfide bonds within the globules, Kramer notes, so perhaps using a different bond avoids potential problems in initial globule formation.
Using fluorescence labelling techniques and thiol-specific reagents the critical free thiol group was localized in the B chain which contains four disulfide bonds.
Results support the involvement of disulfide bonds and noncovalent interactions in the structural arrangement and strengthening of canola protein-k-carrageenan gels.
Three strains from 1968 (Brazil68a, 68c, and 68d) showed a C [right arrow] F substitution at E105, eliminating one of the disulfide bonds that forms the structural architecture of domain 11 (22).
The observation that many of the food allergens are proteins containing intramolecular disulfide bonds that may be important to their allergenicity (Lehrer et al.
Molecular modeling studies have suggested four of these cysteines form two disulfide bonds necessary for furin function.