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Macromolecules

Julia Castellani Biology 4UI English 4.8Average rating 4.8 out of 5 (5 ratings)

Macromolecules

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Macromolecules

  1. Carbohydrates (major energy source)

    • Monomers (Simple)
      • Monosaccharides (C6H12O6)
        • -5 (pentose) or 6 (hexose) carbons
        • Glucose
        • Fructose
          • 2 of carbons are outside of ring
        • Galactose
      • Disaccharides (double sugars)
        • molecules joined by condensation reactions (a water molecule is lost)
        • Maltose (glucose + glucose)
          • -alpha 1-4 linkages -formed by a condensation reaction (lose a water molecule)
        • Sucrose (glucose + fructose)
          • -a.k.a table sugar -most comes from beets
        • Lactose (galactose + glucose)
          • -milk sugar
    • Polysaccharides (Complex)
      • multiple mono/disaccharides join
      • Storage Polysaccharides
        • Starch (plants)
          • -Insoluble -alpha 1-4 linkages
          • Amylose (unbranched)
          • Amylopectin (branched)
        • Glycogen (animals)
          • -insoluble; more branches than amylopectin -stored in liver and muscle tissue (skeletal) -alpha 1-4 + 1-6 linkages
      • Structural Polysaccharides
        • Cellulose (fibre)
          • -linear, unbranched -forms fibrils which reinforce plant cell walls -cannot be digested by animals
        • Chitin
          • -polymer of an amino sugar -makes up exoskeletons -chitin + calcium = hard -semi conductor under certain conditions
  2. Proteins (Polypeptides)

    • -50% of dry weight of cells -"molecular tools" -NATIVE CONFORMATION is the shape in which a protein functions best    -assisted by chaperone proteins -proteins can be DENATURED (unfold and become non-functional) by changes in temp, pH, or salt concentration 
    • Primary Structure (DNA blueprint)
      • -sequence of amino acids -determined by a single gene -peptide bonds
    • Secondary Structure (regular, repeated backbone folding)
      • Alpha Helix (H-bonds b/w every 4th peptide bond)
      • Beta Pleated Sheet (H-bonds b/w polypeptide chains)
    • Tertiary Structure (irregular folding of a polypeptide via R-group interactions)
      • -R-group (side chain) interactions -"Globular proteins" b/c chape is irregular and globular
      • H-bonds
      • Ionic bonds
      • disulfide bridge (covalent)
      • Hydrophobic
    • Quaternary Structure (multiple polypeptides)
      • -weak interactions/disulfide bridges (eg -s-s-) -each polypeptide chain is a SUBUNIT of the protein
  3. Enzymes (catalysts)

    • -reduce activation energy required for a reaction to occur
    • Thermodynamic Laws
      • 1. total amt of energy in the universe is constant 2. Disorder (entropy) in the universe is always increasing
    • Activation Energy
      • amount of energy required to start a reaction
    • Lock and Key Theory
      • -one enzyme (loc) has a specific shape for one set of substrates (key)
    • Induced-Fit Theory
      • -shape of the active site changes somewhat after substrate(s) bind to it
    • Competitive Inhibition
      • -"look-alike" molecule binds to active site -enzyme unable to bind with substrate -enzymes inactivated
      • Penicillin
        • kills succeptible bacteria by inhibiting the enzyme that catalyzes the final step in cell wall biosynthesis
      • ACE Inhibitors
        • Inhibit enzymes that make angiotensin II hormone (constricts blood vessels)
      • Ethanol
        • antidote for methanol poisoning
      • Grapefruit
        • Inhibit a drug-metabolizing enzyme in the small intestine
    • Non-Competitive Inhibition
      • Molecules bind to a site adjacent to active cite and change the shape of the active site
      • Eg) Heavy metals
    • Allosteric Regulation
      • Molecules bind to a site AWAY from active site
      • Allosteric activation
      • Allosteric deactivation
      • Co-enzyme (vitamin aiding enzyme's action)
      • Co-factor (mineral aiding enzyme's action
  4. Lipids (Energy and Structure)

    • -C, O, H (no ratio) -hydrophobic
    • Fats and Oils
      • *Glycerol + 3 Fatty Acid chains *joined by ester linkages
      • Saturated Fatty Acids
        • -solid at room temp *Every carbon bond holds a Hydrogen -eg) animal fats
      • Unsaturated Fatty Acids
        • -liquid at room temp *Some double bonds (more double bonds = healthier)
        • Monounsaturated (1 double bond)
        • Polyunsaturated (more than 1 double bond)
        • Cis isomer (H's on same side)
        • Trans isomer (H's on opposite side)
    • Phospholipids
      • -fat derivitives -important in cell membranes *AMPHIPATHIC (hydrophobic + hydrophillic regions)
      • Hydrophilic head
      • Hydrophobic tails
        • -2 fatty acid chains
    • Sterols
      • -flat ring structure of carbons
      • Cholesterol (most common)
        • -found in cell membranes -makes membranes less permeable
        • High-density Lipoprotein (good)
        • Low-Density Lipoprotein (bad)
  5. Nucleic Acids / Polynucleotides (Structure, Functional)

    • -in nucleus and mitochondria -polymers of nucleotides
    • Nucleotides
      • Consists of:
        • a nitrogen base
          • Pyrimidines (single ring)
            • Thymine (DNA) / Uracil (RNA)
            • Cytosine (DNA & RNA)
          • Purines (double ring)
            • Adenine (DNA & RNA)
            • Guanine (DNA & RNA)
        • a 5-carbon sugar
          • Deoxyribose (DNA)
          • Ribose (RNA)
        • a phosphate group
      • 2 types
        • Deoxyribonucleic Acid
          • -Chemical basis for the gene -found in nuclei of cells
        • Ribonucleic Acid
          • -close copies of genes -found in cytoplasm

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Macromolecules
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