Bio Paper 1

• Monomers


  • glucose
  • amino acids
  • nucleotides
• Polymers


  • starch
  • cellulose
  • glycogen
  • proteins
  • DNA
  • RNA
• Condensation reaction to create polymers


  1. Joining two molecules together

  2. Creating a chemical bond

  3. Removing water
• Hydrolysis reaction to break apart monomers


  1. Breaking of a chemical bond between two molecules

  2. Involves the use of water
• Carbohydrate monosaccharides


  • glucose
  • fructose
  • galactose
• Carbohydrate disaccharides


  • sucrose
  • maltose
  • lactose
• Carbohydrate polysaccharides


  • starch
  • cellulose
  • glycogen
• Alpha glucose


  Hydrogen atom on top, hydroxyl group on bottom of carbon 1
• Beta glucose


  Hydroxyl group on top, hydrogen atom on bottom of carbon 1
• Glycosidic bond


  Chemical bond that forms between two monosaccharides in disaccharides
• Starch


  • Glucose store in plants
  • Made from alpha glucose
• Cellulose


  • Structural strength in plant cell walls
  • Made from beta glucose
• Glycogen


  • Glucose store in animals
  • Made from alpha glucose
  • Highly branched structure
• Triglycerides


  Lipid with 3 fatty acid chains attached to a glycerol molecule
• Phospholipids


  Lipid with 2 fatty acid chains and a phosphate group attached to a glycerol molecule
• Amino acid


  Central carbon, hydrogen, amine group, carboxyl group, variable R group
• Forming a dipeptide


  Condensation reaction to join two amino acids with a peptide bond
• Forming a polypeptide


  Multiple condensation reactions to join many amino acids with peptide bonds
• Primary protein structure


  • Sequence of amino acids in the polypeptide chain
• Secondary protein structure


  • Folding of the polypeptide chain into alpha helices or beta pleated sheets, held by hydrogen bonds
• Tertiary protein structure


  • Further folding of the polypeptide chain into a unique 3D shape, held by ionic, hydrogen and disulfide bonds
• Quaternary protein structure


  • Multiple polypeptide chains assembled together
• Enzymes


  Proteins in the tertiary structure that catalyze reactions by lowering activation energy
• Enzyme active site


  • Unique shape complementary to a specific substrate
• Induced fit model


  Enzyme active site slightly changes shape to mold around the substrate
• Factors affecting enzyme-controlled reaction rate

  • Temperature
  • pH
  • Substrate concentration
  • Enzyme concentration
  • Inhibitors
• Lower temperature


  Fewer successful enzyme-substrate collisions, lower reaction rate
• Temperature above optimum


  Bonds break, enzyme denatures, active site changes, lower reaction rate
• pH away from optimum

  Charges in active site disrupted, enzyme denatures, lower reaction rate
• Insufficient substrate


  Fewer enzyme-substrate collisions, lower reaction rate
• Substrate saturates enzyme active sites


  Reaction rate remains constant even with more substrate
• Insufficient enzyme


  Active sites saturated, lower reaction rate
• Excess enzyme, no more substrate


  Reaction rate remains constant
• Competitive inhibitor


  Binds to the enzyme active site
• Non-competitive inhibitor


  Binds to a different part of the enzyme
• If there's insufficient enzymes, the active sites will become saturated with whatever substrate is there and the rate will stay low
• Adding more enzyme


  The rate will increase
• If you keep adding more and more enzymes but don't add any more substrates, you'll just have a surplus of enzymes and the rate won't increase any further
• Competitive inhibitor


  Binds to the active sites, is the same shape or very similar in shape to the substrate
• Non-competitive inhibitor


  Binds to the allosteric site, causes the active site to change shape