Proteins <ul><li>most diverse and important molecules in </li></ul><ul><li>living organisms </li></ul><ul><li>coded for by...
Types of Proteins <ul><li>Type Example </li></ul><ul><li>Structural tendons, cartilage, hair, nails </li></ul><ul><li>Cont...
<ul><li>Examples: </li></ul><ul><li>enzymes – biological catalysts, speed up reactions  </li></ul><ul><li>immunoglobulins ...
Amino Acids <ul><li>organic molecule made of a central C atom attached to an amino group, carboxyl group, H atom and a R g...
<ul><li>20 different R groups = 20 different a.a. </li></ul><ul><li>simplest a.a., glycine, has H atom for R group </li></...
Essential Amino Acids <ul><li>10 not synthesised by body </li></ul><ul><li>arg, his, ile, leu, lys, met, phe, thr, trp, va...
Peptide Bond <ul><li>Formed by bond between COOH of 1 st  amino acid & NH 2  of 2 nd </li></ul><ul><li>Several amino acids...
Protein Structure <ul><li>Primary Structure  (1 o )   – the particular sequence of amino acids that is the backbone of a p...
<ul><li>Secondary Structure (2 o )  -  coils and folds in polypeptide from H bonds between H and O atoms </li></ul><ul><li...
<ul><li>Tertiary Structure (3 o )  – supercoiling of polypeptide, due to attraction between secondary structures (cysteine...
<ul><li>Quaternary Structure (4 o )  – two or more polypeptides forming a functional protein </li></ul><ul><li>ex haemoglo...
Denaturation <ul><li>proteins can only work under certain temp, pH, salt… </li></ul><ul><li>denaturation changes bonds tha...
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Proteins

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Proteins

  1. 1. Proteins <ul><li>most diverse and important molecules in </li></ul><ul><li>living organisms </li></ul><ul><li>coded for by DNA </li></ul><ul><li>structural building blocks for most living </li></ul><ul><li>functions </li></ul><ul><li>made of long polymer of amino acids </li></ul>
  2. 2. Types of Proteins <ul><li>Type Example </li></ul><ul><li>Structural tendons, cartilage, hair, nails </li></ul><ul><li>Contractile muscles </li></ul><ul><li>Transport haemoglobin, myoglobin </li></ul><ul><li>Storage milk, nuts, seeds </li></ul><ul><li>Hormonal insulin, growth hormone </li></ul><ul><li>Enzyme catalyses cells rxns </li></ul><ul><li>Protection immune response </li></ul>
  3. 3. <ul><li>Examples: </li></ul><ul><li>enzymes – biological catalysts, speed up reactions </li></ul><ul><li>immunoglobulins – protection against foreign microbes, cancer cells </li></ul><ul><li>transport proteins – move things across cell membrane </li></ul><ul><li>hemoglobin – carries oxygen in bloodstream </li></ul><ul><li>fibrin – protein to help blood clot : </li></ul>
  4. 4. Amino Acids <ul><li>organic molecule made of a central C atom attached to an amino group, carboxyl group, H atom and a R group </li></ul>
  5. 5. <ul><li>20 different R groups = 20 different a.a. </li></ul><ul><li>simplest a.a., glycine, has H atom for R group </li></ul><ul><li>R group determines nature of a.a., some are hydrophobic or hydrophilic </li></ul>
  6. 6. Essential Amino Acids <ul><li>10 not synthesised by body </li></ul><ul><li>arg, his, ile, leu, lys, met, phe, thr, trp, val </li></ul><ul><li>Must be obtained from diet </li></ul><ul><li>All in dairy products, meat, fish, eggs </li></ul><ul><li>1 or more missing from grains/vegetables </li></ul><ul><li>Some plants; quinoa, buckwheat, hempseed & amaranth have nearly all </li></ul>
  7. 7. Peptide Bond <ul><li>Formed by bond between COOH of 1 st amino acid & NH 2 of 2 nd </li></ul><ul><li>Several amino acids joined together make up a peptide chain </li></ul>
  8. 8. Protein Structure <ul><li>Primary Structure (1 o ) – the particular sequence of amino acids that is the backbone of a peptide chain or protein </li></ul>
  9. 9. <ul><li>Secondary Structure (2 o ) - coils and folds in polypeptide from H bonds between H and O atoms </li></ul><ul><li>α helix – tight coil stabalized by H bonds </li></ul><ul><li>β-pleated sheet – two polypeptide chains run parallel connected by H bonds </li></ul>
  10. 10. <ul><li>Tertiary Structure (3 o ) – supercoiling of polypeptide, due to attraction between secondary structures (cysteine a.a. attract each other forming disulphide bridges) </li></ul>
  11. 11. <ul><li>Quaternary Structure (4 o ) – two or more polypeptides forming a functional protein </li></ul><ul><li>ex haemoglobin – 4 polypeptide chains, 2 α-chains, 2 β-chains, each surrounding a heme group (contains iron) </li></ul>
  12. 12. Denaturation <ul><li>proteins can only work under certain temp, pH, salt… </li></ul><ul><li>denaturation changes bonds that hold 2 o , 3 o , 4 o changing protein’s function </li></ul><ul><li>Causes: heat, pH, heavy metals </li></ul><ul><li>Examples: cooking food, straightening/curling hair, alcohol denaturing bacteria </li></ul>
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