Noun:

পেপটাইড বন্ড,

peptide bond's Usage Examples:

A peptide bond is an amide type of covalent chemical bond linking two consecutive alpha-amino acids from C1 (carbon number one) of one alpha-amino acid.

The LSU rRNA acts as a ribozyme, catalyzing peptide bond formation.

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

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.

Proline has an unusually conformationally restrained peptide bond due to its cyclic structure with its side chain bonded to its secondary.

proline is likely to adopt the cis isomer of the peptide bond, specifically the X-Pro peptide bond; steric and electronic factors heavily favor the trans.

However thermolysin is also widely used for peptide bond formation through the reverse reaction of hydrolysis.

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

A peptide bond forms between the amino acid attached to the tRNA in the P site and the.

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

retroviral aspartyl protease (retropepsin), an enzyme involved with peptide bond hydrolysis in retroviruses, that is essential for the life-cycle of HIV.

different specificity for their substrate; trypsin, for example, cleaves the peptide bond after a positively charged residue (arginine and lysine); chymotrypsin.

double-bond nature of the peptide bond, a small fraction occurs in cis.

Unlike regular peptide bonds, the X-Pro peptide bond does not adopt the intended.

Endoproteinase Arg-C) is a proteinase that cleaves proteins on the carboxyl peptide bond of arginine.

affects the rate of peptide bond formation between proline and other amino acids.

When proline is bound as an amide in a peptide bond, its nitrogen is not.

translational elongation from the formation of the first to the last peptide bond of a growing polypeptide.

50S includes the activity that catalyzes peptide bond formation (peptidyl transfer reaction), prevents premature polypeptide.

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

be the cleaved bond in the self-cleaving hammerhead ribozyme or the peptide bond of a substrate cleaved by a peptidase.

Additionally, proline can form stable trans-isomers at the peptide bond.

Synonyms:

peptide linkage; bond; chemical bond;

Antonyms:

secured bond; unsecured bond; repulsion; detach;