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Decoding Cancer Progression: Biology and Math Unite

Explore the intersection of biology and mathematics in understanding cancer progression. Dive into the citric acid cycle, electron transport, and oxidative phosphorylation to uncover vital insights. Join us on Feb. 23, 2010, for an enlightening lecture by Alyssa Weaver at Sigma Xi-CST. Framed in an easy-to-follow format, this event promises to shed light on the complexities of cancer evolution. Discover the roles of energy metabolism and electron transfer, as well as the regulatory mechanisms that drive cellular processes. Enhance your knowledge and advance your understanding of cancer dynamics.

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Decoding Cancer Progression: Biology and Math Unite

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  1. Feb 23, 2010 18:30-20:30 - Sigma Xi-CST lecture, Fraser 4 - Understanding Cancer Progression: Bringing Biology and Mathematics to the Challenge Alyssa Weaver Exam W 2/246-8 pm Review W afternoon?

  2. Isotopic Tests: Generation of specifically labeled OAA

  3. +CoASH CH3 CH3- COO- C=O CoASH When in the TCA cycle would this label be lost as CO2?

  4. Table 21-2 Standard Free Energy Changes (DG°¢) and Physiological Free Energy Changes (DG) of Citric Acid Cycle Reactions. Page 790

  5. Figure 21-25Regulation of the citric acid cycle. Page 791

  6. Figure 21-26 Amphibolic functions of the citric acid cycle. Page 793

  7. Chapter 22: Electron Transport and Oxidative Phosphorylation

  8. OH- carbanion • E + H+ + Fum  EH+ + Fum▪OH-E ▪ H+ ▪Mal-   18O exchange E + H+ + Mal

  9. Figure 22-1 The sites of electron transfer that form NADH and FADH2 in glycolysis and the citric acid cycle. Page 798

  10. Figure 22-2a Mitochondria. (a) An electron micrograph of an animal mitochondrion. Page 799

  11. Figure 22-2b Mitochondria. (b) Cutaway diagram of a mitochondrion. Page 799

  12. Figure 22-3 Freeze-fracture and freeze-etch electron micrographs of the inner and outer mitochondrial membranes. Page 799

  13. Figure 22-7 The malate–aspartate shuttle. Page 801

  14. Figure 22-8 The glycerophosphate shuttle. Page 802

  15. Figure 22-9 The mitochondrial electron-transport chain. Page 803

  16. Table 22-1Reduction Potentials of Electron-Transport Chain Components in Resting Mitochondria. Page 806

  17. Table 22-1 (continued) Reduction Potentials of Electron-Transport Chain Components in Resting Mitochondria. Page 806

  18. Table 22-1 (continued) Reduction Potentials of Electron-Transport Chain Components in Resting Mitochondria. Page 806

  19. Table 22-1 (continued) Reduction Potentials of Electron-Transport Chain Components in Resting Mitochondria. Page 806

  20. Figure 22-11 Effect of inhibitors on electron transport. Page 805

  21. Figure 22-12 Electron micrographs of mouse liver mitochondria. (a) In the actively respiring state. (b) In the resting state. Page 806

  22. Figure 22-13 Determination of the stoichiometry of coupled oxidation and phosphorylation (the P/O ratio) with different electron donors. Page 807

  23. Figure 22-14The mitochondrial electron-transport chain. Page 808

  24. Figure 22-15 Structures of the common iron–sulfur clusters. (a) [Fe–S] cluster. (b) [2Fe–2S] cluster. (c)[4Fe–4S] cluster. Page 808

  25. Figure 22-17 Oxidation states of the coenzymes of complex I. (a) FMN. (b) CoQ. Page 810

  26. Figure 22-20 Active site interactions in the proposed mechanism of the QFR-catalyzed reduction of fumarate to succinate. Page 812

  27. Figure 22-21a Visible absorption spectra of cytochromes. (a) Absorption spectrum of reduced cytochrome c showing its characteristic a, b, and g (Soret) absorption bands. Page 813

  28. Figure 22-21Visible absorption spectra of cytochromes.(b) The three separate a bands in the visible absorption spectrum of beef heart mitochondrial membranes (below) indicate the presence of cytochromes a, b, and c. Page 813

  29. Figure 22-22a Porphyrin rings in cytochromes. (a) Chemical structures. Page 813

  30. Figure 22-22b Porphyrin rings in cytochromes. (b) Axial liganding of the heme groups contained in cytochromes a, b, and c are shown. Page 813

  31. Figure 22-25c X-Ray structure of fully oxidized bovine heart cytochrome c oxidase. (c) A protomer viewed similarly to Part a showing the positions of the complex’s redox centers. Page 816

  32. Figure 22-28 Proposed reaction sequence for the reduction of O2 by the cytochrome a3–CuB binuclear complex of cytochrome c oxidase. Page 819

  33. Figure 22-29 Coupling of electron transport (green arrow) and ATP synthesis. Page 821

  34. “Alfonse, Biochemistry makes my head hurt!!” \

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