peptide 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.

pep·tide bond

the common link (-CO-NH-) between amino acids in proteins, actually a substituted amide, formed by elimination of H2O between the -COOH of one amino acid and the H2N- of another. Compare: eupeptide bond, isopeptide bond.

peptide bond

n.
The chemical bond between carboxyl groups and amino groups of neighboring amino acids, forming an amide group and constituting the primary linkage of all protein structures.

pep·tide bond

(pep'tīd bond)
The common link (-CO-NH-) between amino acids in proteins, formed by elimination of H2O between the -COOH of one amino acid and the H2N- of another.

peptide bond

A covalent bond formed between amino acids during protein synthesis. The OH- on a carbon atom links with the H- on a nitrogen atom to form a water molecule which is given off as each peptide bond is formed. Amino acids linked by peptide bonds form dipeptides, tripeptides or polypeptides.
Peptide bondclick for a larger image
Fig. 249 Peptide bond . Molecular structure. R1 R2 distinctive side-chains for different amino acids.

peptide bond

a covalent C arbon-N itrogen bond that joins the carboxyl group of one AMINO ACID to the amino group of another (with loss of a water molecule). See Fig. 249 . Many amino acids are joined by peptide bonds to form a POLYPEPTIDE CHAIN.

pep·tide bond

(pep'tīd bond)
The common link (-CO-NH-) between amino acids in proteins.

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 ?
To prove the theory, Watanabe and his team recreated the formation of peptide bonds in vitro by using a type of ribosomal RNA they created from E.
Alkaline relaxers induce so much damage to African hair not only because they break hydrogen bonds, salt linkages, disulfide bonds, and peptide bonds, but also because a large number of the broken bonds break irreversibly and, as a consequence, the hair fibers lose between 40-60% of their mechanical strength.
The biuret test is a chemical test used for detecting the presence of peptide bonds.
Proteases have roles that extend far beyond a simple catalytic function in the hydrolysis of peptide bonds of proteins.
Peptides are short polymers of amino acid monomers linked together by peptide bonds.
In hair, the keratin in the cortex has peptide bonds and hydrogen bonds that supply strength and elasticity to the cortex and help keep it together.
Detection is based on ultraviolet absorbance at 200 nm (Capillarys, Sebia) or 214 nm (Paragon 2000, Beckman Coulter), which corresponds to the absorption of peptide bonds in proteins.
Doctors must inject peptide drugs rather than give them orally, because digestive enzymes snip peptide bonds.
It is widely used in cell culture research and bioproduction to cleave peptide bonds and to remove adherent cells from surfaces while maintaining cell viability and integrity.
All peptide bonds in short peptides would be available for immediate interaction with copper, as none of the peptide bonds will be buried within a globular structure; no denaturation would be required before interaction with copper.
Hydrolysis is a chemical process where an enzyme is used to break the peptide bonds of a protein, resulting in smaller molecular derivatives called polypeptides and peptides.
The peptide most likely recognizes the catalytic site in intact PSA as it does not recognize PSA inactivated by partial cleavage of certain peptide bonds (15).