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Average = 112.4 = C+

Average = 112.4 = C+. Standard deviation = 16. A = 131+ B- = 113-117 A- = 126-130 C+ = 109-112 B+ = 122-125 C = 96-105 B= 118-121 C- = 85-95. Enzyme Catalysis Chapter 11. Table 11-1. Table 11-2. Figure 11-1. Page 325. Figure 11-2. Page 326. Figure 11-3. Figure 11-4. Page 327.

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Average = 112.4 = C+

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  1. Average = 112.4 = C+ Standard deviation = 16 A = 131+ B- = 113-117 A- = 126-130 C+ = 109-112 B+ = 122-125 C = 96-105 B= 118-121 C- = 85-95

  2. Enzyme Catalysis Chapter 11

  3. Table 11-1

  4. Table 11-2

  5. Figure 11-1

  6. Page 325

  7. Figure 11-2

  8. Page 326

  9. Figure 11-3

  10. Figure 11-4

  11. Page 327

  12. Figure 11-5b

  13. Figure 11-7

  14. Figure 11-12 Biologically Important Nucleophiles and Electrophiles

  15. Box 11-1

  16. Figure 11-9 RNase S complexed with a nonhydrolyzable substrate.

  17. Figure 11-10 Catalytic mechanism of RNase A.

  18. Figure 11-10 part 1

  19. Figure 11-10 part 2

  20. We’re going to skip section 4 in Chapter 11 on lysozyme and continue with section 5: Serine Proteases

  21. Table 15-4 A Selection of Serine Proteases. Page 516

  22. Figure 11-24

  23. Figure 11-25 Trypsin

  24. Figure 11-26

  25. Figure 11-27

  26. Figure 11-28

  27. Figure 11-29

  28. Figure 11-29 Catalytic mechanism ofthe serine proteases. Page 522

  29. Catalytic mechanism of the serine proteases. Page 522

  30. Catalytic mechanism of the serine proteases. Page 522

  31. Catalytic mechanism of the serine proteases. Page 522

  32. Page 522

  33. Catalytic mechanism of the serine proteases. Page 522

  34. Page 522

  35. Figure 11-30a

  36. Figure 11-30b

  37. Figure 15-22 Relative positions of the active site residues in subtilisin, chymotrypsin, serine carboxypeptidase II, and ClpP protease. Page 521

  38. Example of “convergent” evolution.

  39. Figure 11-31 Trypsin and Bovine Pancreatic Trypsin Inhibitor

  40. Figure 11-33

  41. Box 11-4a

  42. Box 11-4b

  43. Box 11-4c

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