g12 sl humanbiochem
TRANSCRIPT
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Introduction
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Energy Proteins Carbohydrates Lipids Micronutrients and Macronutrients Hormones Enzymes (AHL) Nucleic Acids (AHL) Respiration (AHL)
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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)
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Use calorimeter
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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)
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H++ H2N-CHR-COO-← H
3N+-CHR-COO- → H
3N+-CHR-COOH + OH-
>At low pH>Extra H+ reacts with OH-
>[OH- ] drops>Equilibrium shifts to the right>H
3N+-CHR-COOH form
>positive charge
>At high pH>Extra OH- reacts with H+
>[H+] drops>Equilibrium shifts to the left>H
2N-CHR-COO- form
>negative charge
>At isoelectric point>identical ionizations>only zwitterion>H
3N+-CHR-COO- form
>no net charge
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H3N+-CHR-COO- + H+→ H
3N+-CHR-COOH +
H2O
>when H+ is added>equilibrium shifts to right
>[H+] drops>pH remains the same>buffer action
>when OH- is added>equilibrium shifts to left
>[OH-] drops>pH remains the same>buffer action
H2O + H
2N-CHR-COO-← OH- + H
3N+-CHR-COO-
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AminoLeft
AcidRight
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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 chains
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Tertiary structureMyoglobin
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Quaternary structureHaemoglobin
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Structural (collagen, keratin) Catalysts (enzymes) Hormones (insulin) Antibodies (interferons) Transport (haemoglobin) Energy (from muscles)
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distance traveled by compounddistance traveled by solventR
f =
Rf is specific for each amino acid
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H++ H2N-CHR-COO-← H
3N+-CHR-COO- → H
3N+-CHR-COOH + OH-
>At isoelectric point (pH of buffer)>identical ionizations>only zwitterion>H
3N+-CHR-COO- form
>no net charge>not affected by electric field
Different amino acids have different isoelectric points
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Electrophoresis(constant pH)
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