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 ?
In one report (7), the group captured immunoglobulins by using antisera to [kappa] and [lambda] light chains, and then reduced disulfide bonds and scanned for light chains with restricted mlz ratios.
The essential principle of the Erel and Neselioglu method is the reduction of disulfide bonds (S=S) to reactive thiol groups in the presence of NaB[H.
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 Cys288 to Cys326 disulfide bond in domain V can be reduced by oxidoreductase enzymes thioredoxin (TRX-1) and protein disulfide isomerase (PDI).
Interesting research undertaken by Lafont and collaborators [25] showed that the healing efficiency of a thermoset aliphatic epoxy resins with disulfide bonds in its structure depended on the level of crosslinking achieved using trifunctional or tetrafunctional thiols as crosslinking agents.
In platelets, membrane PDI members, such as PDIA1, ERP5, and ERP57, are known for their paramount importance in platelet aggregation through the isomerization of a disulfide bond in the [[alpha].
2]S reduces cysteine disulfide bonds but does not sulfurate cysteine residues.
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).
For example, human epidermal growth factor (hEGF), secreted through the Sec pathway, is properly folded, has disulfide bonds, and is functional, with the same biological level of activity as that of endogenous EGF (Figure 4).
Because plants are able to produce recombinant proteins the same way mammalian cell cultures do, including post-translational modifications like disulfide bonds among others.
NAC will break disulfide bonds, creating two sulfhydryl molecules.
Sulfur is important for supporting disulfide bonds between collagen fibrils helping to preserve the pliancy of our skin," said Rodney Benjamin, technical director for Bergstrom Nutrition.