Macromolecules

1. Monomers (Simple)
   1. Monosaccharides (C6H12O6)

      Anotações:

      • -5 (pentose) or 6 (hexose) carbons
      1. Glucose
      2. Fructose

         Anotações:

         • 2 of carbons are outside of ring
      3. Galactose
   2. Disaccharides (double sugars)

      Anotações:

      • molecules joined by condensation reactions (a water molecule is lost)
      1. Maltose (glucose + glucose)

         Anotações:

         • -alpha 1-4 linkages -formed by a condensation reaction (lose a water molecule)
      2. Sucrose (glucose + fructose)

         Anotações:

         • -a.k.a table sugar -most comes from beets
      3. Lactose (galactose + glucose)

         Anotações:

         • -milk sugar
2. Polysaccharides (Complex)

   Anotações:

   • multiple mono/disaccharides join
   1. Storage Polysaccharides
      1. Starch (plants)

         Anotações:

         • -Insoluble -alpha 1-4 linkages
         1. Amylose (unbranched)
         2. Amylopectin (branched)
      2. Glycogen (animals)

         Anotações:

         • -insoluble; more branches than amylopectin -stored in liver and muscle tissue (skeletal) -alpha 1-4 + 1-6 linkages
   2. Structural Polysaccharides
      1. Cellulose (fibre)

         Anotações:

         • -linear, unbranched -forms fibrils which reinforce plant cell walls -cannot be digested by animals
      2. Chitin

         Anotações:

         • -polymer of an amino sugar -makes up exoskeletons -chitin + calcium = hard -semi conductor under certain conditions

Anotações:

• -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 

1. Primary Structure (DNA blueprint)

   Anotações:

   • -sequence of amino acids -determined by a single gene -peptide bonds
2. Secondary Structure (regular, repeated backbone folding)
   1. Alpha Helix (H-bonds b/w every 4th peptide bond)
   2. Beta Pleated Sheet (H-bonds b/w polypeptide chains)
3. Tertiary Structure (irregular folding of a polypeptide via R-group interactions)

   Anotações:

   • -R-group (side chain) interactions -"Globular proteins" b/c chape is irregular and globular
   1. H-bonds
   2. Ionic bonds
   3. disulfide bridge (covalent)
   4. Hydrophobic
4. Quaternary Structure (multiple polypeptides)

   Anotações:

   • -weak interactions/disulfide bridges (eg -s-s-) -each polypeptide chain is a SUBUNIT of the protein

Anotações:

• -reduce activation energy required for a reaction to occur

1. Thermodynamic Laws

   Anotações:

   • 1. total amt of energy in the universe is constant 2. Disorder (entropy) in the universe is always increasing
2. Activation Energy

   Anotações:

   • amount of energy required to start a reaction
3. Lock and Key Theory

   Anotações:

   • -one enzyme (loc) has a specific shape for one set of substrates (key)
4. Induced-Fit Theory

   Anotações:

   • -shape of the active site changes somewhat after substrate(s) bind to it
5. Competitive Inhibition

   Anotações:

   • -"look-alike" molecule binds to active site -enzyme unable to bind with substrate -enzymes inactivated
   1. Penicillin

      Anotações:

      • kills succeptible bacteria by inhibiting the enzyme that catalyzes the final step in cell wall biosynthesis
   2. ACE Inhibitors

      Anotações:

      • Inhibit enzymes that make angiotensin II hormone (constricts blood vessels)
   3. Ethanol

      Anotações:

      • antidote for methanol poisoning
   4. Grapefruit

      Anotações:

      • Inhibit a drug-metabolizing enzyme in the small intestine
6. Non-Competitive Inhibition

   Anotações:

   • Molecules bind to a site adjacent to active cite and change the shape of the active site
   1. Eg) Heavy metals
7. Allosteric Regulation

   Anotações:

   • Molecules bind to a site AWAY from active site
   1. Allosteric activation
   2. Allosteric deactivation
   3. Co-enzyme (vitamin aiding enzyme's action)
   4. Co-factor (mineral aiding enzyme's action

Anotações:

• -C, O, H (no ratio) -hydrophobic

1. Fats and Oils

   Anotações:

   • *Glycerol + 3 Fatty Acid chains *joined by ester linkages
   1. Saturated Fatty Acids

      Anotações:

      • -solid at room temp *Every carbon bond holds a Hydrogen -eg) animal fats
   2. Unsaturated Fatty Acids

      Anotações:

      • -liquid at room temp *Some double bonds (more double bonds = healthier)
      1. Monounsaturated (1 double bond)
      2. Polyunsaturated (more than 1 double bond)
      3. Cis isomer (H's on same side)
      4. Trans isomer (H's on opposite side)
2. Phospholipids

   Anotações:

   • -fat derivitives -important in cell membranes *AMPHIPATHIC (hydrophobic + hydrophillic regions)
   1. Hydrophilic head
   2. Hydrophobic tails

      Anotações:

      • -2 fatty acid chains
3. Sterols

   Anotações:

   • -flat ring structure of carbons
   1. Cholesterol (most common)

      Anotações:

      • -found in cell membranes -makes membranes less permeable
      1. High-density Lipoprotein (good)
      2. Low-Density Lipoprotein (bad)

Anotações:

• -in nucleus and mitochondria -polymers of nucleotides

1. Nucleotides
   1. Consists of:
      1. a nitrogen base
         1. Pyrimidines (single ring)
            1. Thymine (DNA) / Uracil (RNA)
            2. Cytosine (DNA & RNA)
         2. Purines (double ring)
            1. Adenine (DNA & RNA)
            2. Guanine (DNA & RNA)
      2. a 5-carbon sugar
         1. Deoxyribose (DNA)
         2. Ribose (RNA)
      3. a phosphate group
   2. 2 types
      1. Deoxyribonucleic Acid

         Anotações:

         • -Chemical basis for the gene -found in nuclei of cells
      2. Ribonucleic Acid

         Anotações:

         • -close copies of genes -found in cytoplasm