Peptide bond

Definition

A peptide bond is a covalent chemical bond formed between two amino acid molecules. It occurs when the carboxyl group of one amino acid reacts with the amino group of another, releasing a molecule of water.

5 Must Know Facts For Your Next Test

1. Peptide bonds are essential for forming proteins, linking amino acids into polypeptide chains.
2. The formation of a peptide bond is a dehydration synthesis reaction, also known as a condensation reaction.
3. Peptide bonds are planar and rigid, contributing to the structural stability of proteins.
4. The breaking of peptide bonds through hydrolysis is crucial in protein digestion and degradation processes.
5. In RNA translation, peptide bonds are formed in the ribosome during protein synthesis.

Review Questions

• What type of reaction leads to the formation of a peptide bond?
• Why are peptide bonds important for protein structure?
• Where does the formation of peptide bonds occur during protein synthesis?

Related terms

Amino Acid:

Organic compounds that combine to form proteins and consist of an amino group, carboxyl group, and side chain.

Polypeptide:

A polymer consisting of many amino acids linked by peptide bonds.

Ribosome:

The cellular machinery where RNA is translated into proteins via the formation of peptide bonds.