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AP Biology Biochemistry Unit Review Questions

AP Biology Biochemistry Unit Review Questions. 1. Is this molecule polar/ nonpolar? Explain why. 2 . Is this molecule polar/ nonpolar? Explain why. Draw a molecule of water. Identify the regions that are positive and negative.

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AP Biology Biochemistry Unit Review Questions

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  1. AP BiologyBiochemistry UnitReview Questions

  2. 1. Is this molecule polar/ nonpolar? Explain why.

  3. 2. Is this molecule polar/ nonpolar? Explain why.

  4. Draw a molecule of water. Identify the regions that are positive and negative.

  5. Add one molecule of water to your drawing. Show how it would form a hydrogen bond with the first molecule of water.

  6. Sketch how Water would surround a chloride ion (Cl-).

  7. Describe what property of water allows this. Explain what is happening at the molecular level.

  8. Dehydration Synth or Hydrolysis?

  9. Endergonic/ Exergonic?

  10. Catabolic/ Anabolic?

  11. Stores/ Releases Energy?

  12. Shown below is a generic amino acid. Sketch two in the correct positions on opposite sides forming peptide bonds.

  13. Based off of your sketch, describe what kind of reaction has occurred and what has happened energetically?

  14. List the levels of protein structure and give a brief description of each.

  15. Dehydration synthesis causes amino acids to form peptide bonds at this level(s) of protein structure.

  16. The three-dimensional shape of the protein is formed by this level(s) of protein structure

  17. Which Level of protein structure?

  18. Which Level of protein structure?

  19. Which Level of protein structure?

  20. Which Level of protein structure?

  21. A protein is located in the cell surrounded by water. Where would a nonpolar amino acid side chain be located in this protein?

  22. Use Table 3.2 In the book. Amino acid # 137 is Tryptophan. Which substitution would cause the greatest disruption in protein structure? Provide Reasoning.A. LeucineB. GlycineC. Tyrosine

  23. What is denaturation?Identify the factors that can cause denaturation?

  24. How do enzymes work? • Sketch a graph to help illustrate your explanation.

  25. Enzyme Structure • Sketch a generic enzyme and its substrate. • Label the active site • Put a star by a location where a competitive inhibitor would bind. • Put a triangle by a location where the allosteric regulator would bind.

  26. Sketch a graph that shows the change in reaction rate with increased enzyme concentration. (Assume substrate concentration is unlimited.)

  27. Sketch a graph that shows how the reactions rate is affected by increased substrate concentration (assume limited enzyme concentration).

  28. Compare/ contrast cofactors with coenzymes

  29. What are the two types of natural inhibitors/ regulators for enzymes? • What do they have in common?

  30. Compare/ contrast competitive inhibitors with allosteric inhibitors. • Compare/ contrast and allosteric inhibitor with an allosteric activator.

  31. What type of regulation? • A molecule weakly binds at the active site, preventing the substrate from binding.

  32. What type of regulation? • A molecule weakly binds to an enzyme and introduces a hydrophobic side chain that cause the 3-D shape of the protein to change. This results in exposure of the active site and enzyme function. • What is the purpose of this type of regulation?

  33. What type of regulation? • A molecule weakly binds to an enzyme and causes the 3-D shape of the protein to change. This results in loss of the shape of the active site.

  34. Describe what’s happening below:

  35. What happens if enzyme 3 is inhibited?

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