Noun:

पेप्टाइड बंध,

peptide bond's Usage Examples:

peptidase that catalyzes the cleavage of the terminal (or the penultimate) peptide bond; the process releases a single amino acid or dipeptide from the peptide.

28) is a protease found in picornaviruses, which cleaves peptide bonds of non-terminal sequences.

18) is a protease enzyme that hydrolyzes (cleaves) a peptide bond at the carboxy-terminal (C-terminal) end of a protein or peptide.

aspartic acid residue act respectively as proton donor and proton acceptor, catalysing the hydrolysis of peptide bond in proteins.

The result of this sequential cascade is to bind ubiquitin to lysine residues on the protein substrate via an isopeptide bond, cysteine residues.

is able to act as a nucleophile, attacking the carbonyl carbon of the scissile peptide bond of the substrate.

Antibiotic targetThe following protein synthesis inhibitors target peptidyl transferase:Chloramphenicol binds to A2451 and A2452 residues in the 23S rRNA of the ribosome and inhibits peptide bond formation.

Both proteins are believed to catalyze peptide bond formation and help resolve ribosomal stalls, making them elongation factors.

activity that catalyzes peptide bond formation (peptidyl transfer reaction), prevents premature polypeptide hydrolysis, provides a binding site for the G-protein.

It is located in the large ribosomal subunit, where it catalyzes the peptide bond formation.

proteins, fragment proteins by cleaving peptide bonds, and synthesize cyanamides and other molecules.

member of this antibiotic class, chloramphenicol, acts by inhibiting peptide bond formation, with recent 3D-structural studies showing two different binding.

It is located in the large ribosomal subunit, where it catalyzes the peptide bond formation.

Synonyms:

peptide linkage, bond, chemical bond,

Antonyms:

secured bond, unsecured bond, repulsion, detach,