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WINTER CAREER FAIR Thursday, February 12, 2004 10:00 a.m. 3:00 p.m.

WINTER CAREER FAIR Thursday, February 12, 2004 10:00 a.m. 3:00 p.m. Viking Union Multi-purpose Room. It's time for the students to submit their request for Chem/Biol 475. Please have them pick up an override form from the Chemistry Office. Submission deadline is February 13, 2004.

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WINTER CAREER FAIR Thursday, February 12, 2004 10:00 a.m. 3:00 p.m.

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  1. WINTER CAREER FAIR Thursday, February 12, 2004 10:00 a.m. 3:00 p.m. Viking Union Multi-purpose Room

  2. It's time for the students to submit their request for Chem/Biol 475. Please have them pick up an override form from the Chemistry Office. Submission deadline is February 13, 2004. What advanced biochem elective would you take next winter? Virology? Something else? Immunolgy?

  3. Feb. 4 : “Optimizing the Design for Observing Chemical • Kinetics in Situ: The Telomerase Reaction” • Dr. George Czerlinski, Research Associate, • Department of Biology, WWU • Synopsis: Dr. Czerlinski will discuss a fluorescence-based assay • using a chemical relaxation jump to study the initial reaction of • telomerase, an enzyme which regulates the integrity of • chromosome ends.

  4. Feb. 11: “Is Intelligent Design a Scientific Alternative to • Darwinism?” • Dr. David Leaf, Department of Biology, WWU • Synopsis: Dr. Leaf will examine the scientific claims of key • biologists in intelligent design, and will discuss the socio-political • agenda of this movement. • Feb. 18: “Mathematical Modeling of Drosophila Development” • 4:00Dr. Mary Anne Pultz, Department of Biology, WWU • Synopsis: Dr. Pultz will discuss her recent work on developing a • mathematical model of the gene network regulating embryonic • patterning in drosophila. • Feb. 25: “Summer Internships” Candace Adamo, Kim Carpenter • & Alisa Milner, Biology Undergraduates, WWU • Synopsis: Alisa, Kim, and Candace will give short presentations • about their summer research internships at Rosetta Inpharmatics, • Amgen and the UC-Riverside NSF REU program.

  5. Figure 20-14 Alternating conformation model for glucose transport. Page 734

  6. Figure 20-15 Regulation of glucose uptake in muscle and fat cells. Page 735

  7. Figure 20-16a X-Ray structure of the KcsA K+ channel.(a) Ribbon diagram. Page 736

  8. Figure 20-16b X-Ray structure of the KcsA K+ channel.(b) A cutaway diagram viewed similarly to Part a. Page 736

  9. Figure 20-16c X-Ray structure of the KcsA K+ channel.(c) A schematic diagram. Page 736

  10. Figure 20-18 Uniport, symport, and antiport translocation systems. Page 739

  11. Figure 20-19 Putative dimeric structure of the (Na+–K+)–ATPase indicating its orientation in the plasma membrane. Page 739

  12. Figure 20-20 Reaction of [3H]NaBH4 with phosphorylated (Na+–K+)–ATPase. Page 740

  13. E1 has inward facing high-affinity Na+ binding site and reacts with ATP to form E1-P when Na+ is bound. E2-P has an outward-facing high-affinity K+ binding site and hydrolyzes to form Pi and E2 only when K+ is bound

  14. Mechanism: 1. E1-3Na+ binds ATP to form a ternary complex • Complex reacts to from the high energy P • intermediate. • Intermediate relaxes to form E2-P-3Na+ and • releases Na+ outside. 4. E2-P binds 2K+ outside to form E2-P-2K+. 5. P is hydrolyzed leavind E2-2K+. • E2-2K+ changes conformation, releasing potassium • ions and replacing them with sodium ions.

  15. Figure 20-21 Kinetic scheme for the active transport of Na+ and K+ by (Na+–K+)–ATPase. Page 741

  16. Figure 20-28 The Na+–glucose symport system represented as a Random Bi Bi kinetic mechanism. Page 748

  17. Figure 20-27ab Glucose transport in the intestinal epithelium. Page 747

  18. Figure 20-27c Glucose transport in the intestinal epithelium. Page 747

  19. Figure 20-25 Transport of glucose by the PEP-dependent phosphotransferase system (PTS).Driven by PEP hydrolysis. Synthesis stimulated by cAMP His containing phosphocarrier protein Page 745 [Presence of glc decreases [cAMP} Substrates modified during transport.

  20. A resting neuron has a negative charge. That is, there are more negative ions inside the axon than outside the axon. (Ions are molecules with an electric charge.) In contrast, the fluid outside the axon has a positive charge. Because the outside and inside of the axon have different charges, the axon is said to be polarized.

  21. When a neuron is excited or fires, several events take place to create an electrical impulse. Sodium ions, which have a positive charge, enter the axon. This depolarizes the axon-that is, changes the electrical charge inside the axon from negative to positive. This change starts at one end of the axon and continues all the way to the other end. In response to this electrical impulse (called an action potential), the vesicles swarm to the very edge of the axon and release neurotransmitters into the synapse. After the neurotransmitters are released, potassium ions flow out of the axon. Potassium ions have a positive charge, so their absence restores the negative charge inside the axon. The neuron is again polarized and at rest, waiting to fire another impulse.

  22. Cool start http://www.rnceus.com/meth/Introneurotrans.html Animation http://www.utexas.edu/research/asrec/neurotr_copy01a.mov Tutorial and Animation http://www.enl.umassd.edu/InteractiveCourse/rstahl/neurotrans. html#actionpotential

  23. Figure 20-33a Time course of an action potential. (a) The axon membrane undergoes rapid depolarization, followed by a nearly as rapid hyperpolarization and then a slow recovery to its resting potential. A wave of transient membrane depolarization Page 753

  24. Figure 20-33b Time course of an action potential. (b) The depolarization is caused by a transient increase in Na+ permeability (conductance), the hyperpolarization results from a more prolonged increase in K+ beginning a fraction of a millisecond later. These result from the presence of sodium and potassium specific voltage-gated channels Page 753

  25. Figure 20-34 Action potential propagation along an axon. One increasing value triggers the next change in potential in an adjacent membrane patch. Page 754

  26. Figure 20-35b Myelination—increasees impulse velocity. (b) A schematic diagram of a myelinated axon in longitudinal section, indicating that in the nodes of Ranvier, the axonal membrane is in contact with the extracellular medium. Page 755

  27. Figure 20-36 The simultaneous depolarization (red, right) of the innervated membranes in a stack of electroplaques “wired” in series results in a large voltage difference between the two ends of the stack. Page 757

  28. Figure 20-39 A selection of neurotransmitters. Page 760

  29. Figure 20-37a Electron crystal structure of the nicotinic acetylcholine receptor from the electric fish Torpedo marmorata. (a) Side view with the synaptic side up. ACh R is a ligand-gated cation channel. Page 758

  30. Figure 20-37b Electron crystal structure of the nicotinic acetylcholine receptor from the electric fish Torpedo marmorata. (b) View into the synaptic entrance of the channel. Page 758

  31. Figure 20-38 X-Ray structure of acetylcholinesterase (AChE). Page 759

  32. Figure 20-29 Kinetic mechanism of lactose permease in E.coli. Page 749

  33. Figure 20-23 Kinetic mechanism of Ca2+–ATPase. Page 742

  34. Figure 20-24aX-Ray structure of the Ca2+–ATPase from rabbit muscle sarcoplasmic reticulum. (a) A tube-and-arrow diagram. Page 743

  35. Figure 20-24bX-Ray structure of the Ca2+–ATPase from rabbit muscle sarcoplasmic reticulum. (b) A schematic diagram of the structure viewed similarly to Part a. Page 743

  36. Figure 20-32 Composite model of the KV channel. Page 751

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