1 / 66

Seminar W 4 pm BI 234 Dr. K. Cude!!

Seminar W 4 pm BI 234 Dr. K. Cude!!. A novel NF  b pathway in the regulation of theG2/M phase of the cell cycle. Refreshments at 3:45 pm….Be there!!!. Many conformational states. Fewer conformational states. See VVP Fig 6-37 p153. A “single” conformational state. “Ideal”.

tavia
Download Presentation

Seminar W 4 pm BI 234 Dr. K. Cude!!

An Image/Link below is provided (as is) to download presentation Download Policy: Content on the Website is provided to you AS IS for your information and personal use and may not be sold / licensed / shared on other websites without getting consent from its author. Content is provided to you AS IS for your information and personal use only. Download presentation by click this link. While downloading, if for some reason you are not able to download a presentation, the publisher may have deleted the file from their server. During download, if you can't get a presentation, the file might be deleted by the publisher.

E N D

Presentation Transcript


  1. Seminar W 4 pm BI 234 Dr. K. Cude!! A novel NFb pathway in the regulation of theG2/M phase of the cell cycle Refreshments at 3:45 pm….Be there!!!

  2. Many conformational states Fewer conformational states See VVP Fig 6-37 p153 A “single” conformational state

  3. “Ideal” “Real” ? See VVP Fig 6-38 p154

  4. High energy Many conformational states Fewer conformational states (Fig 6-38) A “single” conformational state Low energy

  5. H-bond Fun Facts • 1984 survey of protein crystal data shows that “almost all groups capable of forming H-bonds do so.” (mainchain amides, polar sidechains)

  6. VVP Fig 6-39 Take Note p 61

  7. Protein Explorer http://molvis.sdsc.edu/protexpl/frntdoor.htm Do the “1 hour tour” at this site. http://molvis.sdsc.edu/protexpl/qtour.htm It may take longer than 1 h.

  8. Mb

  9. Exploring collagen http://www.rcsb.org/pdb/molecules/pdb4_1.html

  10. Globular Protein 3o Structure 2o structural elements (helices, sheets, turns…) pack together to give a folded protein or subunit. This so-called “tertiary” structure is stabilized by non-covalent interactions, the hydrophobic effect and disulfides. Within the 3o structure are “motifs” and “domains”. The 3o structure can be derived from one or more domains.

  11. Structural features of most globular proteins: 1. Very compact: e.g. Mb has room for only4 water molecules in its interior. 2. Most polar/charged R groups are on the surface and are hydrated. 3. Nearly all the hydrophobic R groups are on the interior. 4. Pro occurs at bends/loops/random structures and in sheets

  12. Figure 8-63 The quaternary structure of hemoglobin. Page 266

  13. Oxygen is transported to cells which are remote from air • O2 is required in cells, in the mitochondria for ATP production aerobic metabolism Glucose + O2 ----------------------------> ATP + CO2 oxidative phosphorylation

  14. Normal Red Blood Cells have a flattened discoid shape rather than a spherical shape O2 O2 O2 O2 O2 O2 O2 O2 O2 O2 O2 vs. O2 O2 O2 O2 O2 O2 O2 O2 O2 O2 O2 O2 O2 O2 O2

  15. Oxygen is transported to cells which are remote from air • O2 is required in cells, in the mitochondria for ATP production aerobic metabolism Glucose + O2 ----------------------------> ATP + CO2 oxidative phosphorylation

  16. Oxygen is transported down a concentration gradient pO2 torr

  17. Transport of O , CO , H + 2 2 See VVP Fig 7-13 p173 lungs BPG.CO . Hb + 4O <===> Hb.(O ) + CO + BPG H . H + + + BPG.CO . Hb + 4O <===> Hb.(O ) + CO + BPG H . H + + + 2 2 2 4 2 2 2 2 4 2 O CO H , + 2 2 tissues Hb.(O ) + CO + BPG <===> BPG.CO . Hb + 4O H + H . + + Hb.(O ) + CO + BPG <===> BPG.CO . Hb + 4O H + H . + + 2 4 2 2 2 2 4 2 2 2 muscle cell membrane Mb O <===> Mb.O + Mb O <===> Mb.O + 2 2 2 2 mitochondria Mb.O <===> Mb O + Mb.O <===> Mb O + 2 2 2 2

  18. VVP Fig 7-1

  19. VVP Fig 7-3 heme myoglobin proximal His (bound to Fe)

  20. VVP Fig 7-2 “proximal His”

  21. P50 = 2.8 torr VVP Fig 7-4

  22. Fraction of Mb bound to O2 at pO2 = 30 torr pO2 in capillaries P50 = 2.8 torr

  23. myoglobin = single subunit hemoglobin = four homologous subunits: two alpha; two beta chains

  24. VVP Fig 7-7

  25. VVP Fig 7-5a

  26. VVP Fig 7-5b

  27. Deoxy-Hb “T State” Oxy-Hb “R State” VVP Fig 7-5

  28. VVP Fig 7-7

  29. VVP Fig7-7 Take Note p 65 Non-cooperative binding Cooperative binding

  30. VVP Fig7-7 Take Note p 65 About 33% of O2 delivered

  31. VVP Fig7-7 Take Note p 65 About 42% of O2 delivered

  32. VVP Fig 7-8

  33. VVP Fig 7-9

  34. VVP Fig 7-10

  35. 4O2 + Hb-BPG-CO2-H+ Hb-(O2)4+ BPG + CO2 +H+ BPG + CO2 +H+ + Hb-(O2)4 Hb-BPG-CO2-H++ 4O2 O2 +Mb Mb-O2 Binding and Release of: O2, BPG, CO2, H+ See VVP Fig 7-13 Lungs: Capillaries: CO2 Respiring cells: Mitochondrion(O2) + Mb

  36. VVP Fig. 7-14 Take Note p 69

  37. Take Note p 69

  38. Take Note p 68

  39. b H146 is deprotonated in the R state b H146

  40. The R to T transition brings b D94 close to b H146. How does this affect pKa for b H146? b H146 b D94 NH CO

  41. How does this affect pKa for b H146? pKa for b H146increases, the protonated state is now favored. b H146 b D94 NH CO

  42. VVP Fig 7-15

  43. adaptation to high altitude: increased [BPG]

  44. Take Note p 378 VVP Fig 27-7

  45. Like VVP Fig 7-15

  46. Ser Ser

More Related