Explain formation of peptide linkage in protein with an example.

Question: Explain formation of peptide linkage in protein with an example.

A peptide linkage is formed when the carboxyl group (-COOH) of one amino acid reacts with the amino group (-NH2) of another amino acid, releasing a molecule of water (H2O) in a process called dehydration synthesis or condensation reaction. The resulting covalent bond between the two amino acids is called a peptide bond. This process is repeated multiple times to create a peptide chain, which can ultimately fold into a protein. For example, in the dipeptide Glycine-Alanine, the carboxyl group of Glycine (-COOH) reacts with the amino group of Alanine (-NH2), releasing a molecule of water and forming a peptide bond (-CO-NH-) between the two amino acids. This reaction can continue to add additional amino acids to the chain to form a longer polypeptide or protein.

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