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 ?
Even though the average spacing between amide groups is the same in nylon 6 as it is in nylon 6/6, the nylon 6/6 has a melting point approximately 40 [degrees]C higher and is slightly stronger and stiffer than nylon 6 because of details in the molecular spacing that are beyond the scope of this article.
1] (the adsorption of MMA units hydrogen-bonded to amide groups is shown as a shoulder at 1720 [cm.
alpha]])of dry and solvent-saturated PA66 samples and mass intake [DELTA] m (referred to the total PA66 mass) and molar intake [DELTA] n (referred to the amount of amide groups in the amorphous phase) of the studied solvents at room temperature (20 [degrees] C).
These results confirm the hydrogen bonding interaction between the amide group and urethane groups of PA6 fiber and CPU thin film coating.
A comparison of the grafting content; mpm (mole of reacted monomer per million part of PP); and chlorine content of the resultant fibers; mpm; indicates that only 12-20% of the amide groups in the grafted NTBA side chains was transformed into N-halamines during chlorination (--NHR [right arrow]--NRCl).
The formation of hydrogen bonds between amide groups of PA1212 and urethane groups or ester groups of TPU during melt processing may increase the compatibility between TPU and PA1212.
liq]) reacts with amino functions N to amide groups A:
This trend may be due to the diluent effect of the soft segment on the crystallizable MCPA6 portion, which could be attributed to the interaction of hydrogen bonding between the urethane groups in the TPEU and the amide groups of MCPA6 [22, 23].
Aliphatic polyamides, named nylons, present three basic crystal structures at room temperature according to the differences in the disposition of the amide groups and the methylene concentration in the repeat unit, based on the classification by Kinoshita in 1959 [1].
The ester groups in the main chains ensure chain susceptibility to enzymes and microbes, and amide groups increase intermolecular forces and improve the thermal and mechanical properties of the final products.
Deshpande developed polymers with allylic or benzylic amide groups covalently bonded to the polymer molecules.
The conversion of protein amide groups to carboxyl groups by deamidation improves solubility and other physical properties of proteins under mildly acidic conditions.