🧬

MCAT Biochemistry: Amino Acids Overview

Apr 27, 2025

MCAT Biochemistry Series: Amino Acids, Peptides, and Proteins

Introduction

  • Presenter: Iman
  • Objective: Start a new series on biochemistry focusing on amino acids, peptides, and proteins for the MCAT.
  • Format: Review chapter content and solve practice problems.

Proteins: Functions and Importance

  • Proteins account for more than 50% of dry mass in cells.
  • Functions:
    • Speed up chemical reactions (enzymes)
    • Defense against invaders (immune function)
    • Storage
    • Transport
    • Cellular communication
    • Structural support
  • Enzymes: Proteins that act as catalysts, lowering activation energy and speeding up reactions.
  • Structural complexity: Proteins have unique 3D shapes.

Amino Acids: Building Blocks of Proteins

  • 20 amino acids form proteins.
  • Amino acids are linked by peptide bonds to form polypeptides.
  • Amino acid structure:
    • Central carbon
    • Amino group (NH2)
    • Carboxyl group (COOH)
    • Hydrogen
    • Variable side chain (R group)
  • Side chains (R groups) determine properties and functions.
  • Categories:
    • Electrically charged side chains
    • Polar vs nonpolar
    • Hydrophobic vs hydrophilic

Memorization Tips

  • Know the structure, three-letter code, and one-letter code for each amino acid.
  • Use flashcards and frequent drawing for memorization.

Special Cases

  • Glycine: Not chiral (two hydrogens attached to central carbon).
  • Cysteine: R configuration, unlike others which are S.
  • Proline: Causes kinks in polypeptide chains.

Acid-Base Chemistry of Amino Acids

  • Amino acids can accept or donate protons.
  • Ionizable groups:
    • Gain protons under acidic conditions, lose them under basic conditions.
    • Low pH: Protonated; High pH: Deprotonated
  • PKA value: pH at which half of the molecules are deprotonated.
  • All amino acids have at least two PKA values for the amino and carboxyl groups.
  • Third PKA for some amino acids with ionizable side chains.

Titration Curves and Isoelectric Point

  • Titration curves demonstrate dissociation constants.
  • Isoelectric point (pI) is the pH where net charge is zero.
  • Formula: pI = (pka1 + pka2) / 2
  • Henderson-Hasselbalch equation relates pH, pKa, and concentration ratios.

Peptide Bond Formation

  • Formed by dehydration reaction.
  • Polypeptides have N-terminus (free amino group) and C-terminus (free carboxyl group).
  • Peptide bonds are stable due to resonance.

Protein Structures

  • Primary Structure: Linear sequence of amino acids.
  • Secondary Structure: 3D structures like alpha helices and beta sheets due to interactions in the chain.
  • Tertiary Structure: Overall 3D conformation due to side chain interactions.
  • Quaternary Structure: Arrangement of multiple polypeptides or subunits.

Conclusion

  • In the next session, practice problems related to this chapter will be tackled.
  • Encouragement for further study and memorization.