peptide bond


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Related to peptide bond: Dipeptide bond

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.
References in periodicals archive ?
Kostic, "Selective hydrolysis of unactivated peptide bonds, promoted by platinum(II) complexes anchored to amino acid side chains," Inorganic Chemistry, vol.
We initially evaluated the variability of both valence bond geometry and peptide bond planarity in the Ramachandran space using a recent database of protein structure (see Methods for details).
Ciurak, "[sup.1]H- and [sup.13]C-nmr investigations on cis-trans isomerization of proline peptide bonds and conformation of aromatic side chains in H-Trp-[(Pro).sub.n]-Tyr-OH peptides," Journal of Biopolymers, vol.
In this method, copperions form a complex in the alkaline environment with protein peptide bonds and the copper is reduced.
(ii) Peptide bonds constitute the representation of an edge graph by linking two amino acids as in Figure 2, which is a representation graph of connected two typical amino acids into an edge graph.
We argue that salt bridges between tails and between heads, mediated, respectively, by cations and anions, are alternatives to peptide bonds, the preferred bond in pure water, thus favouring radial and longitudinal nanotube growth.
The degree of hydrolysis (DH) is defined as the ratio of the number of peptide bonds hydrolyzed to the total number of peptide bonds per unit weight present in HSPP.
Where [h.sub.tot] is the total number of peptide bonds per protein equivalent, and h is the number of hydrolyzed bonds.
Each molecule of protein is made up of many amino acids linked together by strong peptide bonds into one or more polypeptide chains.
Functionally, proteolytic enzymes break peptide bonds in proteins with "varying degrees of specificity".
Peptide bonds are constrained by the LINCS algorithm [75] and water geometries are constrained by SETTLE [76].
Each is active only against the peptide bonds in protein molecules that have carboxyl groups donated by certain amino acids.