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BIBC 102 ANNOUNCEMENTS

BIBC 102 ANNOUNCEMENTS. Randy ’ s bipartite office hours Tue 2 :30 -3:30 pm Wed 2:30-3:30 pm 2130 Pacific Hall. BIBC 102 Web Site. http://courses.ucsd.edu/rhampton/bibc102/. Soft Reserves lecture slides are available. Near Hi Thai. . BIBC 102 ANNOUNCEMENTS. BIBC 102 ANNOUNCEMENTS.

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BIBC 102 ANNOUNCEMENTS

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  1. BIBC 102 ANNOUNCEMENTS Randy’s bipartite office hours Tue 2:30-3:30 pm Wed 2:30-3:30 pm 2130 Pacific Hall BIBC 102 Web Site http://courses.ucsd.edu/rhampton/bibc102/ Soft Reserves lecture slides are available. Near Hi Thai.

  2. BIBC 102 ANNOUNCEMENTS

  3. BIBC 102 ANNOUNCEMENTS Principles of Biochemistry,6th ed Lehninger, Nelson and Cox Will be on reserve at the Biomedical Library, but not Geisel Library

  4. Activation energy and reaction rate fig 6-2

  5. Activation energy and reaction rate fig 6-3

  6. What is the relation between changes in activation energy and reaction rate?

  7. Activation energy and reaction rate k dS/dt = k[S] S P blue terms are constant when temperature is constant...

  8. Activation energy and reaction rate designate blue terms as constants

  9. Activation energy and reaction rate call DG‡ = A for simplicity

  10. Lowering activation energy …

  11. Lowering activation energy … the rate constant is increased by this factor: note the following features: lowering DG‡ makes reaction faster identical effect on both directions when DG‡ is lowered by this amount:d

  12. how big a deal is this? recall thatC2= RT at body temp, RT= 2573 J/mole so if DG‡changes by the value of one hydrogen bond (~20 kJ/mole) rate enhancement is e7.8 = 2440

  13. If you have not already please read LIGAND BINDING and ENZYME CATALYSIS

  14. If you have not already please read LIGAND BINDING and ENZYME CATALYSIS

  15. Ligand Binding rh

  16. Does this form make intuitive sense? when there is no L, LB is also 0 as L gets big, LB approaches B saturable rh

  17. Binding isotherm rectangular hyperbola rh

  18. Enzyme kinetics: binding and beyond when there is no S, reaction rate is 0 as S gets big, rate reaches a maximum saturable rh

  19. Maud Menten VmaxS Vo = Km + S Michaelis-Menten Equation again, a rectangular hyperbola rh

  20. VmaxS Vo = Km + S Michaelis-Menten Equation when there is no S, V0 is also 0 as S gets big, V0 approaches Vmax saturable rh

  21. fig 6-11

  22. how fast can an enzyme “do” a reaction? Vmax = kcat[E]T table 6-7

  23. Competition for binding remember to tell them about I and Y feature of saturability rh

  24. action of a competitive enzyme inhibitor fig 6-15

  25. action of a uncompetitive inhibitor fig 6-15

  26. a “suicide” inhibitor catalytic action of enzyme causes permanent covalent inhibition fig 6-16

  27. CHYMOTRYPSIN: a protease

  28. CHYMOTRYPSIN: a protease fig 6-18

  29. catalytic triad fig 6-21

  30. fig 6-21

  31. fig 6-21

  32. fig 6-21

  33. fig 6-21

  34. fig 6-21

  35. fig 6-21

  36. fig 6-21

  37. fig 6-21

  38. amprenavir Agenerase® Why do we need these details? an example: The HIV Protease: cleaves single HIV-encoded polypeptide into various proteins needed for viral replication Specific inhibitors of the HIV protease were developed by an intimate understanding of the structure and mechanism of the enzyme

  39. Now many HIV protease inhibitors fig 6-30

  40. amprenavir in HIV protease active site

  41. hexokinase reaction pg 212

  42. hexokinase fig 6-22

  43. hexokinase induced fit fig 6-22

  44. site of Pi transfer fig 6-22

  45. C6 ATP ATP glucose transfer of P from ATP xyulose hydrolysis of ATP

  46. Regulation by phosphorylation: general case fig 6-35

  47. Regulation by phosphorylation: general case switchable changes in activity can activate or diminish activity

  48. phosphorylation of glycogen phosphorylase dephosphorylated enzyme less active phosphorylated enzyme more active fig 6-36 ish

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