G12 sl humanbiochem

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G12 sl humanbiochem

  1. 1. Introduction
  2. 2.  Energy Proteins Carbohydrates Lipids Micronutrients and Macronutrients Hormones Enzymes (AHL) Nucleic Acids (AHL) Respiration (AHL)
  3. 3.  We derive our energy from the oxidation of food  Fats (37 kJ g-1)  Carbohydrates  CO2 + H2O + energy  Proteins (17 kJ g-1) Males have a RDI of 10500 kJ, females 8000 kJ Lipids have a greater ratio of H:O than carbohydrates (16:1 compared to 2:1)
  4. 4.  Use calorimeter
  5. 5.  Natural polymers made by amino acids.  Proteins important to humans are made of 20 α-amino acids (in data booklet)  Essential amino acids: amino acids our body cannot synthesize (10)  Complete protein: a protein made of essential amino acids, e.g. casein (milk, eggs, soybeans)Jan 3, 2010 Human Biochemistry 9
  6. 6. Jan 3, 2010 Human Biochemistry 10
  7. 7. Jan 3, 2010 Human Biochemistry 11
  8. 8. Jan 3, 2010 Human Biochemistry 12
  9. 9. Jan 3, 2010 Human Biochemistry 13
  10. 10. >At isoelectric point >identical ionizations >only zwitterion >H3N+-CHR-COO- form >no net chargeH++ H2N-CHR-COO-← H3N+-CHR-COO- → H3N+-CHR-COOH + OH->At high pH >At low pH>Extra OH- reacts with H+ >Extra H+ reacts with OH->[H+] drops >[OH- ] drops>Equilibrium shifts to the left >Equilibrium shifts to the>H2N-CHR-COO- form right>negative charge >H3N+-CHR-COOH form >positive chargeJan 3, 2010 Human Biochemistry 14
  11. 11. >when H+ is added H3N+-CHR-COO- + H+→ H3N+-CHR-COOH +>equilibrium shifts to right H O 2>[H+] drops>pH remains the same>buffer action>when OH- is added H2O + H2N-CHR-COO-← OH- + H3N+-CHR-COO>equilibrium shifts to left>[OH-] drops>pH remains the same>buffer action Jan 3, 2010 Human Biochemistry 15
  12. 12. Jan 3, 2010 Human Biochemistry 16
  13. 13. Amino Acid Left RightJan 3, 2010 Human Biochemistry 17
  14. 14. Primary structure >sequence of amino acids >characteristic of protein function Secondary structure >folding of polypeptide chain >by Hydrogen bonds α-helix: between atoms of the same chain, e.g. hair, wool pleated sheet: between parallel chains, e.g. silk random coil: no repeating pattern Tertiary structure >3D shape of secondary structure > several types of interaction Quaternary structure >3D shape of tertiary structures of different polypeptide chainsJan 3, 2010 Human Biochemistry 18
  15. 15. Jan 3, 2010 Human Biochemistry 19
  16. 16. Tertiary structure MyoglobinJan 3, 2010 Human Biochemistry 20
  17. 17. Quaternary structure HaemoglobinJan 3, 2010 Human Biochemistry 21
  18. 18. Jan 3, 2010 Human Biochemistry 22
  19. 19. Jan 3, 2010 Human Biochemistry 23
  20. 20.  Structural (collagen, keratin)  Catalysts (enzymes)  Hormones (insulin)  Antibodies (interferons)  Transport (haemoglobin)  Energy (from muscles)Jan 3, 2010 Human Biochemistry 24
  21. 21. Jan 3, 2010 Human Biochemistry 25
  22. 22. distance traveled by compound Rf = distance traveled by solvent Rf is specific for each amino acidJan 3, 2010 Human Biochemistry 26
  23. 23. >At isoelectric point (pH of buffer) >identical ionizations >only zwitterion >H3N+-CHR-COO- form >no net charge >not affected by electric fieldH++ H2N-CHR-COO-← H3N+-CHR-COO- → H3N+-CHR-COOH + OH- Different amino acids have different isoelectric pointsJan 3, 2010 Human Biochemistry 27
  24. 24. Electrophoresis (constant pH)Jan 3, 2010 Human Biochemistry 28
  25. 25. Jan 3, 2010 Human Biochemistry 29

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