TOPIC 1

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  • TOPIC 1
    • Carbohydrates
      • Monosaccharides - OH Bellow on Alpha, Above on Beta
      • Disaccharides - glycosidic bonds
        • C-O-C
      • Polysaccharides - Multiple carbohydrate molecules joined together through glycosidic bonds
        • Starch - a-glucose amalose 1-4 bonds, amylopectin 1-4 & 1-6 bonds (branching)
        • Glycogen - a-glucose like amylopectin but more frequent 1-6 branches
        • Cellulose - B-glucose lie next to each other, alternative inversion allowing hydrogen bonding.
    • Lipids
      • hydrophobic acids made from fatty acids and glycerol
      • Triglycerides - 3 fatty acids, 1 glycerol molecule- synthesized during condensation reaction.
      • Functions - large long term energy stores. - waterproofing and insulating
        • Phospholipids- phosphate and glycerol = head and fatty acid = tails
    • Proteins
      • Amino Acids
      • Peptide Bonds
      • STRUCTURE
        • TERTIARY - A helix or B pleated sheets
        • SECONDARY - how polypeptide chains are held together
        • QUATERNARY - different chains held together
        • PRIMARY - sequence of amino acids
      • HAEMOGLOBIN - globular, found in red blood cells, $ subunits joined by an oxygen
      • COLLAGEN - fibrous. gives strength to tissues, tendons and skin, 3 a helixes and hydrogen bonds.
    • Nucleic Acids
      • phosphate attached to pentose sugar and attached to a nitrogenous base
      • phosphodiester bonds
      • mRNA = CODON, tRNA = ANTICODON
      • DNA Replication: 1- helicase unzips 2- RNA primae adds RNA sequences 3- DNA Polymerase III adds nucleotides to strands in 5' to 3' direction 4- lagging strand = okazaki fragments 5- DNA Polymerase I removes RNA primers 6- DNA Ligase joins okazaki fragments together
    • Protein Synthesis
      • Transcription: 1- starts at promoter region 2- mRNA made from template strand RNA Polymerase moves along making mRNA 3- hairpin loop forms 4- mRNA leaves nucleus to get to the cytoplasm
      • Translation: 1- ribosomes assembles the 30s unit then the 50s unit 2- AUG (start codon)  binds to P site 3- tRNA binds to A site , peptide bond formed between amino acids 4- tRNA exits E site
      • Mutation- Substitution: one amino acid is changed Deletion: remove an amino acids Insertion: add an amino acid
        • SICKLE CELL ANEMIA - glutamic acid changes to valine (GAG>GUG) less efficent to carry CO2
    • Enzymes
      • Highly Specific, each substrate is specific to the enzyme
        • Induced Fit, substrate changes shape to fit the active site
      • Competetive Inhibition
        • Non-Competitive Inhibition
          • End Product Inhibition
    • Water
      • Dipole Nature
        • Properties - highly specific heat capacity H bonds  - High surface tension H bonds - incompressible - maximum density at 4C (ice floats)
  • Factors affecting enzyme:  Temperature, pH, Substrate conc, Enzyme conc

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