SBI4U - Metabolic Processes

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Oddishii
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284308
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SBI4U - Metabolic Processes
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2014-09-29 06:46:15
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grade 12 poop biology sbi4u bellissimo
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  1. Define metabolism
    Chemical reactions occurring in an organism
  2. Define catabolism
    • Breaking down
    • Larger molecules to smaller molecules
    • Complex to simple
    • Releases energy
  3. Define anabolism
    • Building up
    • Smaller molecules to bigger molecules
    • Simple to complex
    • Stores energy
  4. What are buffers?
    Buffers resists significant changes in pH levels; keeps acid and bases in equillibrium
  5. Name the subunits of the following:
    Carbohydrates
    Proteins
    Lipids
    Nucleic Acid
    • Simple sugars
    • Amino Acids
    • Glycerol and fatty acids
    • Nucleotides
  6. What is a condensation/dehydration synthesis reaction?
    • This reactions takes out an H from one unit and a OH from another unit, forming a water molecule. Monomers would be attached using dehydration synthesis. 
    • Simple -> complex
    • Energy is absorbed
    • Anabolic
    • Covalently bonded molecules is the result
  7. This reactions takes out an H from one unit and a OH from another unit, forming a water molecule. Monomers would be attached using this reaction
    Condensation/dehydration synthesis
  8. What is a hydrolysis reaction?
    • This reaction adds H2O, breaking it into H and OH and adding it to a polymor, breaking it down to monomers
    • Complex -> simple
    • Energy is released
    • Catabolic
    • Two unites are resulted
  9. 1:2:1 ratio of C:H:O
    Carbohydrates
  10. This carb contains a single carbon chain attached to –OH
    Monosaccharides
  11. Do simple sugars form chains in water
    yas
  12. What connects simple sugars to form an oligosaccharide?
    Glycosidic linkages
  13. Starch
    Energy storing

    Produced by plants through photosynthesis

    Consists of amylose (straight chained a-glucose 1-4 linkage) and amylopectin (branched chain a-glucose polymer 1-4 and 1-6 linkages)
  14. Glycogen
    energy storing

    “Animal starch”

    • Excess glucose stored as glycogen in liver and
    • muscles

    When concentration of glucose is low, glycogen will be hydrolyzed

    Stores small amounts and will be depleted in a day if not replenished
  15. Cellulose
    structure

    Produced by plants

    Straight chains of b glucose held together by B 1-4 glycosidic bonds H bonds

    Most abundant organic compound

    • Humans lack enzymes to break down B 1-4
    • glycosidic bonds
  16. Name the glycosidic linkage that holds cellulose together
    b 1-4
  17. What element does chitin have that cellulose does not?
    N
  18. Why are fats nonpolar?
    Less OH bonds; less electronegative therefore not soluble in water but soluble in other nonpolar solutions
  19. How are fatty acids and glycerol connected?
    Ester linkages
  20. What is the difference between saturated and unsaturated fats?
    • Saturated fats have only single bonds and solid bc straight hydrocarbons can stack nicely; unsaturated have double bonds and
    • liquid bc bent so less Van der Waals attractions
  21. What are phospholipids a special type of fat?
    Composed of glycerol molecule attached to two fatty acids and a highly polar phosphate group (head very polar and hydrophilic; tail nonpolar and hydrophobic)
  22. What are sterols made of?
    four hydrocarbon rings
  23. What are waxes made of?
    long chain fatty acids linked to alcohols or carbon rings
  24. Which protein is not amphiprotic?
    Proline; it makes a nonpolar covalent bond with its R group
  25. Why are proteins so diverse?
    20 R groups and the four levels of protein structure
  26. Name some functions of proteins
    Transport, Enzymes, Antibodies, Clotting, Hormones, Extra, Receptors, Structure
  27. Primary Structure
    o    Sequence of amino acids directed by DNA when protein synthesis occurs

    o    Protein synthesis is when amino acids are added to the growing chain

    o    BONDING CHARACTERISTIC: covalent peptide bonds
  28. Secondary Structure
    o    Pleating or coiling of the primary structure due to H bonding between carboxyl and amino acids repeatedly

    o    Results in a helix (e.g. keratin) or b pleated sheets (e.g. silk) (this occurs when two parts of the polypeptide chain lie parallel to one another, hydrogen bonding on the adjacent strand)

    o    BONDING CHARACTERISTIC: hydrogen bonding
  29. Tertiary Structure
    • o    3D shape of proteins occur due to various interactions
    • (LD, DD, H-Bond) occurring in R groups :

    • §  Hydrophobic reactions – directing themselves to
    • core of proteins

    §  H-bonds – between polar R-Groups

    §  Ionic bonds – between + and – charged R groups

    • §  Disulfide bridges – covalent bonds occurring in
    • sulfhydryl groups (strongest)

    o    Chaperone proteins help structural formation
  30. Name the types of bonds between R groups in the tertiary structure
    • Hydrophobic 
    • H-Bond - polar
    • Ionic - charged
    • Disulfide - sulfhydryl groups
  31. Quarternary Structure
    • 2 or more polypeptides to produce shape of
    • proteins
  32. Summarize the four levels of structure of a protein
    • Primary is amino acids building together
    • Secondary is amino acids making long chains of itselves
    • Tertiary is R groups attaching to R groups
    • Quaternary is everyone
  33. Name four factors of denaturation
    §  Heat

    §  pH

    §  ion charge

    §  immersion in organic solvents
  34. Name ways denaturation is used
    Spoiling bacteria

    Blanching fruits denatures browning enzymes

    Temporarily straightening hair

    Gastrin denatured by pH of intestine

    Meats easier to chew bc proteins denatured
  35. What is DNA missing?
    Hydroxyl group on carbon 2
  36. In DNA, what always lines up?
    Each strand of DNA has a free phosphate group at one end and a free sugar on the other end = phosphate and sugar always line up
  37. What does RNA do?
    Read info
  38. What is cAMP?
    Second messenger of hormones
  39. In an endothermic potential energy diagram, what would have more energy: products, or reactants? Is energy stored or released?
    Products have more energy; energy is stored
  40. In an exothermic potential energy diagram, what would have more energy: products, or reactants? Is energy stored or released?
    Reactants have more energy; energy is released
  41. What factors cause entropy?
    • Change of state
    • Diffusion
    • More moles
    • Complex -> simple
  42. For an increse in entropy, what is favoured: exothermic or endothermic?
    Exothermic
  43. Explain the concept of free energy
    Free energy is energy that can do useful work. The entropy of the universe increases with any change, even apparently orderly changes have an even greater disorder caused by energy yielding catabolic processes. This disorder makes useful work.
  44. Reversible reactions are possible, however if it reaches an equilibrium of 0, free enegy is 0. That can mean a dead cell. How do cells avoid this?
    Cells makes reactions into long series in which a product can be a reactant of another reaction, with the end product being waste.
  45. Describe the ATP cycle of life
    ATPase hydrolyzes the ATP terminal phosphate to create ADP with an inorganic phosphate, releasing 31 kJ/mol (54 kJ/mol in a living cell), enough to make free energy to drive endergonic processes. However, to make sure this energy doesn't come off as heat, killing the cell, the iorganic phosphate attaches to another molecule through phosphorylation
  46. What are factors afecing enzyme action?
    • ·        
    • Enzyme
    • concentration: the more, the higher the rate of reaction

    • ·        
    • Substrate
    • concentration: the more, the higher the rate of reaction

    • ·        
    • Temperature:
    • only to a certain optimal point before it denatures and rate goes down

    • ·        
    • pH:
    • only to a certain optimal point before it denatures and rate goes down
  47. How do cofactors and coenzymes work together?
    help enzymes function by binding to active sites with covalent bonds, or binding weakly with substrate
  48. What's the difference between competitive and non-competitive inhibition?
    Competitve takes the actual active site; noncompetive takes an allosteric site to change conformation and affinity

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