ib BIOCHEM OPTION

    Cards (96)

    • define metabolism
      chemical reactions that occur in living organism
    • Anabolic
      Building up, from monomers to polymers
    • Catabolic
      Breaking down, from polymers to monomers
    • Metabolic pathways

      1. Monomers join to form polymers
      2. Water is released (condensation)
      3. Polymers break down into monomers
      4. Water is required (hydrolysis)
    • Anaerobic conditions

      Produce lactic acid, ethanol, and other products with less energy compared to aerobic conditions
    • Breaking down insulin protein to amino acids
      Hydrolysis - water goes in to break the bonds
    • Amino acids

      Monomers that make up proteins
    • Amino group

      Part of amino acid structure
    • Carboxylic acid group

      Part of amino acid structure
    • Isoelectric point
      pH at which an amino acid has no net charge
    • Amphoteric
      Amino acids that can act as both acids and bases
    • Protein formation

      1. Amino acids form peptide bonds
      2. Peptide bonds form primary structure
      3. Primary structure forms secondary structure (alpha helix, beta sheet)
      4. Secondary and tertiary structures form quaternary structure
    • Fibrous proteins

      • Primarily have secondary structure
      • Insoluble
    • Globular proteins

      • Have complex tertiary and quaternary structure
      • Soluble
    • Protein analysis
      1. Break proteins into amino acids
      2. Detect amino acids by chromatography or electrophoresis
    • Retardation factor (Rf)

      Ratio of distance moved by amino acid to distance moved by solvent in chromatography
    • Ninhydrin
      Toxic chemical used to detect amino acids in chromatography
    • Enzymes
      Proteins that catalyse chemical reactions by providing an active site that lowers the activation energy
    • Enzymes
      • Highly specific shape that fits substrate
      • Increase reaction rates by millions of times
    • Increasing temperature

      Disrupts hydrogen bonds in protein tertiary structure, causing denaturation
    • Changing pH

      Excess H+ or OH- disrupts protein tertiary structure, causing denaturation
    • Heavy metals

      Bind to sulfhydryl groups in proteins, disrupting tertiary structure
    • Cofactors that are vitamins are called coenzymes
    • Inorganic catalysts are more stable but less specific and slower than enzymes
    • Biological molecules

      • Proteins
      • Lipids
      • Carbohydrates
      • Nucleic acids
    • Van der Waals forces

      Nonpolar, insoluble
    • Types of lipids

      • Triglycerides
      • Phospholipids
      • Steroids
    • Ester
      Chemical linkage between glycerol and fatty acids
    • Ketones, esters, ethers
      Chemical groups
    • Condensation
      1. Water coming out
      2. How glycerol and fatty acids combine
    • Hydrolysis
      How glycerol and fatty acids break up
    • Triglycerides
      • 14-22 carbons long
      • Even number
      • Saturated if no double bonds
      • Unsaturated if double bonds
    • Saturated fats have straight lines, stick together, higher melting/boiling point due to London dispersion forces
    • Unsaturated fats have kinks, less surface area, lower melting/boiling point
    • Omega-3, omega-6

      Refers to the carbon number where the double bond occurs
    • Saturated vs unsaturated fats

      Saturated more likely to be solid, unsaturated more likely to be liquid
    • Iodine number

      Measure of unsaturation - number of grams of iodine that will react with 100g of fat
    • Iodine number determination

      1. Iodine reacts with double bonds
      2. Excess iodine reacts with thiosulfate
      3. Calculations to determine iodine number
    • Unsaturated fats like olive and soybean oil have high iodine numbers, saturated animal fats have low iodine numbers
    • Rancidity
      1. Hydrolysis by water, enzymes, acids
      2. Oxidation by oxygen, free radicals, sunlight
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