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Biomolecules: Amino Acids and
Peptides
Lecture 4, Medical Biochemistry
Lecture 4 Outline
• Present and discuss the properties of amino
acids
• Discuss the importance of pKa values and
amino aci...
At physiological pH’s (7.0-7.4), both
the carboxyl and amino groups are
charged
Only L-amino
acids are
found in
proteins
Non-protein Amino Acids
Examples of Clinical
Aminoacidurias
• Metabolic defects: Phenylketonuria (Phe),
Tyrosinemias (Phe,Tyr), Maple Syrup Urine
...
Post-translational Modifications
BONDPEPTIDE
Resonance forms of peptide bonds.
The peptide bond (C) is a hybrid of A and B,
giving it a partial double bond character
Planar nature of the peptide bond. The
partial double bond characteristic prevents
free rotation around the C-N bond; keep...
Trans conformation;
most common and
sterically favored
Cis conformation;
found rarely with Pro,
sterically unfavorable
The planar nature of the peptide
bond restricts the possible
conformations that a protein
can assume. This can be
predicte...
Levels of Protein Structure
Biomolecules: Amino Acids and Peptides
Biomolecules: Amino Acids and Peptides
Biomolecules: Amino Acids and Peptides
Biomolecules: Amino Acids and Peptides
Biomolecules: Amino Acids and Peptides
Biomolecules: Amino Acids and Peptides
Biomolecules: Amino Acids and Peptides
Biomolecules: Amino Acids and Peptides
Biomolecules: Amino Acids and Peptides
Biomolecules: Amino Acids and Peptides
Biomolecules: Amino Acids and Peptides
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Lecture 4: Medical Biochemistry, Biomolecules: Amino Acids and Peptides

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Biomolecules: Amino Acids and Peptides

  1. 1. Biomolecules: Amino Acids and Peptides Lecture 4, Medical Biochemistry
  2. 2. Lecture 4 Outline • Present and discuss the properties of amino acids • Discuss the importance of pKa values and amino acid titration curves • NOTE: Ignore the techniques section in your book chapter 4 (p. 33-34)
  3. 3. At physiological pH’s (7.0-7.4), both the carboxyl and amino groups are charged Only L-amino acids are found in proteins
  4. 4. Non-protein Amino Acids
  5. 5. Examples of Clinical Aminoacidurias • Metabolic defects: Phenylketonuria (Phe), Tyrosinemias (Phe,Tyr), Maple Syrup Urine Disease (Leu, Val, Ile), Alcaptonuria (Tyr) • Absorption/transport defects: cystinuria (Cys), Hartnup disease , Fanconi’s Syndrome • These diseases are generally diagnosed from indicators in the urine or plasma. These diseases will be discussed further in the amino acid metabolism lectures
  6. 6. Post-translational Modifications
  7. 7. BONDPEPTIDE
  8. 8. Resonance forms of peptide bonds. The peptide bond (C) is a hybrid of A and B, giving it a partial double bond character
  9. 9. Planar nature of the peptide bond. The partial double bond characteristic prevents free rotation around the C-N bond; keeping it in the same plane with the attached O and H atoms. These planar bonds can pivot around the shared Cα atom
  10. 10. Trans conformation; most common and sterically favored Cis conformation; found rarely with Pro, sterically unfavorable
  11. 11. The planar nature of the peptide bond restricts the possible conformations that a protein can assume. This can be predicted by the angle (above or below the peptide bond plane) of the two bonds between the α-carbon of the constituent amino acids. These phi (φ) and psi (ψ) angles can be used to predict and define some higher order protein structures. Peptide Bond Steric Restrictions
  12. 12. Levels of Protein Structure
  • ShivamPandey263

    Sep. 18, 2020
  • FirngizRstmli

    Apr. 29, 2020
  • BataliLokere

    Feb. 23, 2020

Lecture 4: Medical Biochemistry, Biomolecules: Amino Acids and Peptides

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