Campbell 8.4 - 8.5 Quiz

20 Questions | Total Attempts: 229

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Campbell 8.4 - 8.5 Quiz - Quiz

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Questions and Answers
  • 1. 
    Explain Fig. 8.13 in your own words.  Be sure to highlight ALL starred portions discussed in class.
  • 2. 
    Describe the main idea of the first paragraph on p.155 on the topic of how substrate concentration affects reaction rate when an enzyme is present.
  • 3. 
    The name of the enzyme shown in the very first diagram in 8.4 is ____________________. (the diagram showing the hydrolysis of sucrose).
  • 4. 
    The reaction profiled in Fig. 8.12 must be an ___________________ reaction since it has a negative deltaG.
  • 5. 
    Molecule C-D is a reactant of the reaction shown in Fig. 8.12.
    • A. 

      True

    • B. 

      False

  • 6. 
    _________________________ is the energy needed to start a reaction.
  • 7. 
    The size of the activation energy will determine the rate of a reaction since it determines how much energy investment is needed for the reaction to proceed.
    • A. 

      True

    • B. 

      False

  • 8. 
    Enzymes cannot change the deltaG of a reaction - they can only speed a reaction that would occur anyway.
    • A. 

      True

    • B. 

      False

  • 9. 
    Enzymes are extremely specific to their ________________ because of their precise 3-D (tertiary) shapes.  Even very similar molecules will not fit into an enzyme's active site.
  • 10. 
    Check any of the following that WOULD change if a reaction proceeded with vs. without an enzyme.
    • A. 

      Reactants

    • B. 

      Products

    • C. 

      Ea

    • D. 

      DeltaG (free energy change)

    • E. 

      Rate of reaction

  • 11. 
    The _____________________ is the precise place on an enzyme that a substrate will bind.
  • 12. 
    Every enzyme has an _________________ temperature and pH at which its 3D shape is most perfect and therefore at which it works best.
  • 13. 
    Check any of the following that are disrupted if the temperature of a reaction gets TOO hot.
    • A. 

      Hydrogen bonds

    • B. 

      Covalent bonds

    • C. 

      Van der waals interactions

    • D. 

      Ionic bonds

  • 14. 
    Initially, raising the temperature of an enzyme-catalyzed reaction slightly will speed the reaction rate because it causes more _______________ between enzymes and substrates as the molecules move around more.
  • 15. 
    See Fig. 8.16 A.  The difference between the optimal temperature of a typical human enzyme and that of a thermophilic bacteria is ________ degrees Celcius.
  • 16. 
    See Fig. 8.16 B.  Pepsin works best at basic pHs and trypsin works best at acidic pHs.
    • A. 

      True

    • B. 

      False

  • 17. 
    _______________________, like vitamins, can bind to enzymes and help them to work.
  • 18. 
    An ___________________ would be like the opposite of a cofactor since it would bind to an enzyme and DECREASE its ability to function.
  • 19. 
    ____________________ inhibitors bind in the active site of the enzyme and therefore prevent the substrate from binding.
  • 20. 
    _____________________ inhibitors don't bind in the active site - they bind to another place on the enzyme that causes its 3D shape to change and therefore prevents the substrate from binding.
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