Peptide Linkage

Peptide linkage refers to the bond CONH found in proteins, which is formed between the carboxyl group of one amino acid and the amino group of another amino acid.

Structure

- The peptide bond is a covalent bond that forms between the carbon atom of the carboxyl group (C=O) of one amino acid and the nitrogen atom of the amino group (NH2) of another amino acid.
- This bond formation involves the removal of a water molecule, a process known as dehydration synthesis.

Importance

- Peptide linkages are crucial for the structure and function of proteins. Proteins are made up of long chains of amino acids linked together by peptide bonds.
- The sequence of amino acids in a protein determines its unique structure and function.

Characteristics

- Peptide bonds are very stable and resistant to hydrolysis.
- They have partial double bond character, which restricts rotation around the bond and contributes to the rigidity of the protein structure.

Function

- Peptide linkages play a vital role in the formation of the primary structure of proteins.
- They are responsible for holding together the amino acid residues in a specific sequence, which ultimately determines the overall structure and function of the protein.

In conclusion, the bond CONH is known as a peptide linkage and plays a fundamental role in the structure and function of proteins.