B1.2.2 - Condensation reactions forming dipeptides and longer chains of amino acids

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Last updated 7:13 PM on 10/17/26
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4 Terms

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Condensation ⁣Reaction of Linking Amino Acids

  • Amino acid + ‌Amino acid → Dipeptide + Water

  • Amino acids join ‍end-to-end through condensation reactions.

  • The bond that forms ‍between the remaining carbon and nitrogen is called a peptide bond.‍

  • It is a strong covalent bond.

  • Two amino acids linked by ‌a single peptide bond form a dipeptide.




<ul><li><p><strong>Amino acid + ‌Amino acid → Dipeptide + Water</strong></p></li><li><p>Amino acids join ‍end-to-end through <strong>condensation reactions</strong>.</p></li><li><p>The bond that forms ‍between the remaining carbon and nitrogen is called a <strong>peptide bond</strong>.‍</p></li><li><p>It is a strong <strong>covalent bond</strong>.</p></li><li><p>Two amino acids linked by ‌a single peptide bond form a <strong>dipeptide</strong>.</p></li></ul><p><br></p><p></p>
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Dipeptides ‍and Polypeptides

  • The process does not stop at ‍two amino acids.

  • Each additional amino acid is added by another ‍condensation reaction, extending the chain and releasing another water ‌molecule.

  • Short chains (fewer than about 20 amino acids) are ‌called oligopeptides.

  • Longer chains are called polypeptides, and these ‍fold into functional proteins.

  • Every polypeptide has two distinct ends.

    1. The ‌N-terminus has a free amino group (-NH₂).

    2. The C-terminus ‌has a free carboxyl group (-COOH).

    3. The chain always runs ‍from N-terminus to C-terminus, giving it a defined direction.


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Hydrolysis

  • The reverse of condensation is ‍hydrolysis.

  • A water molecule is added across the peptide bond, ‍breaking it and releasing the individual amino acids.

  • Hydrolysis is ‍how your body breaks down dietary protein during digestion.


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Backbone ‌and R Groups

  • The repeating sequence of atoms along the chain ‍(N-C-C-N-C-C...) forms the polypeptide backbone.

  • This backbone ‍is identical in every polypeptide.

  • What makes each polypeptide unique ‌is the sequence of R groups that project outward from the ‌backbone.

  • The R groups determine the chemical properties of the ‌polypeptide and drive how it folds into its final three-dimensional shape.‍