Peptide Bond Formation
The final section explains the formation of peptide bonds, which is the fundamental process in protein synthesis.
Key points about peptide bond formation:
- Two amino acids react through a condensation reaction, releasing a water molecule.
- The peptide bond forms between the carboxyl group of one amino acid and the amino group of another.
- The resulting molecule is called a dipeptide.
Vocabulary: Condensation reaction - A reaction in which two molecules combine to form a larger molecule, typically with the loss of a small molecule such as water.
The document describes the structure of a peptide, including:
- N-terminal end
- C-terminal end
- Peptide bond
Highlight: The peptide bond is very stable, while the terminal ends can react further to form longer chains.
Classification of peptide chains:
- Oligopeptides: 2 to 9 amino acid residues
- Polypeptides: 10 to 100 amino acid residues
- Proteins: more than 100 amino acid residues
This information is crucial for understanding how individual amino acids come together to form the complex structures of proteins, which are essential for numerous biological functions.
Example: The dipeptide formed by alanine and glycine is shown, illustrating the peptide bond formation process.
The document also mentions mesomeric boundary formulas, which help explain the planar nature and partial double bond character of the peptide bond. This structural feature is critical for understanding higher-order protein structures.
