OPTION B: Human Biochemistry B2: Proteins. Objectives Jan 3, 2010 B.2.1 Draw the general formula of 2-amino acids B.2.2 Describe the characteristic properties.

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OPTION B: Human Biochemistry B2: Proteins

Objectives Jan 3, 2010 B.2.1 Draw the general formula of 2-amino acids B.2.2 Describe the characteristic properties of 2- amino acids. B.2.3 Describe the condensation reaction of 2-amino acids to form polypeptides B.2.4 Describe and explain the primary, secondary, tertiary structure of proteins. B.2.5 Explain how proteins can be analysed by chromatography and electrophoresis. B.2.6 List the major functions of proteins in the body.

 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, 2010Human Biochemistry3

Jan 3, 2010Human Biochemistry4

Jan 3, 2010Human Biochemistry5

Jan 3, 2010Human Biochemistry6

Jan 3, 2010Human Biochemistry7

Jan 3, 2010Human Biochemistry8 H + + H 2 N-CHR-COO - ← H 3 N + -CHR-COO - → H 3 N + -CHR-COOH + OH - >At low pH >Extra H + reacts with OH - >[OH - ] drops >Equilibrium shifts to the right >H 3 N + -CHR-COOH form >positive charge >At high pH >Extra OH - reacts with H + >[H + ] drops >Equilibrium shifts to the left >H 2 N-CHR-COO - form >negative charge >At isoelectric point >identical ionizations >only zwitterion > H 3 N + -CHR-COO - form > no net charge

Jan 3, 2010Human Biochemistry9 H 3 N + -CHR-COO - + H + → H 3 N + -CHR-COOH + H 2 O >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 H 2 O + H 2 N-CHR-COO - ← OH - + H 3 N + -CHR-COO -

Jan 3, 2010Human Biochemistry10

Jan 3, 2010Human Biochemistry11 Amino Left Acid Right

Jan 3, 2010Human Biochemistry12 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

Jan 3, 2010Human Biochemistry13

Jan 3, 2010Human Biochemistry14 Tertiary structure Myoglobin

Jan 3, 2010Human Biochemistry15 Quaternary structure Haemoglobin

Jan 3, 2010Human Biochemistry16

Jan 3, 2010Human Biochemistry17

Structural (collagen, keratin) Catalysts (enzymes) Hormones (insulin) Antibodies (interferons) Transport (haemoglobin) Energy (from muscles) Jan 3, 2010Human Biochemistry18

Jan 3, 2010Human Biochemistry19

Jan 3, 2010Human Biochemistry20 distance traveled by compound distance traveled by solvent R f = R f is specific for each amino acid

Jan 3, 2010Human Biochemistry21 H + + H 2 N-CHR-COO - ← H 3 N + -CHR-COO - → H 3 N + -CHR-COOH + OH - >At isoelectric point (pH of buffer) >identical ionizations >only zwitterion > H 3 N + -CHR-COO - form > no net charge >not affected by electric field Different amino acids have different isoelectric points

Jan 3, 2010Human Biochemistry22 Electrophoresis (constant pH)

Jan 3, 2010Human Biochemistry23