WINTER CAREER FAIR

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WINTER CAREER FAIR Thursday, February 12,
2004 1000 a.m. 300 p.m. Viking Union
Multi-purpose Room
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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?
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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.
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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 400 Dr. 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.
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Figure 20-14 Alternating conformation model for
glucose transport.
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Figure 20-15 Regulation of glucose uptake in
muscle and fat cells.
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Figure 20-16a X-Ray structure of the KcsA K
channel.(a) Ribbon diagram.
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Figure 20-16b X-Ray structure of the KcsA K
channel.(b) A cutaway diagram viewed similarly
to Part a.
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Figure 20-16c X-Ray structure of the KcsA K
channel.(c) A schematic diagram.
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Figure 20-18 Uniport, symport, and antiport
translocation systems.
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Figure 20-19 Putative dimeric structure of the
(NaK)ATPase indicating its orientation in the
plasma membrane.
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Figure 20-20 Reaction of 3HNaBH4 with
phosphorylated (NaK)ATPase.
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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
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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.

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Figure 20-21 Kinetic scheme for the active
transport of Na and K by (NaK)ATPase.
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Figure 20-28 The Naglucose symport system
represented as a Random Bi Bi kinetic mechanism.
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Figure 20-27ab Glucose transport in the
intestinal epithelium.
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Figure 20-27c Glucose transport in the
intestinal epithelium.
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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
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Presence of glc decreases cAMP
Substrates modified during transport.
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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.
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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.
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Cool start http//www.rnceus.com/meth/Introneurotr
ans.html
Animation http//www.utexas.edu/research/asrec/neu
rotr_copy01a.mov
Tutorial and Animation http//www.enl.umassd.edu/I
nteractiveCourse/rstahl/neurotrans. htmlactionpot
ential
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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
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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
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Figure 20-34 Action potential propagation along
an axon. One increasing value triggers the next
change in potential in an adjacent membrane patch.
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Figure 20-35b Myelinationincreasees 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.
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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.
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Figure 20-39 A selection of neurotransmitters.
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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.
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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.
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Figure 20-38 X-Ray structure of
acetylcholinesterase (AChE).
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Figure 20-29 Kinetic mechanism of lactose
permease in E.coli.
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Figure 20-23 Kinetic mechanism of Ca2ATPase.
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Figure 20-24aX-Ray structure of the Ca2ATPase
from rabbit muscle sarcoplasmic reticulum. (a) A
tube-and-arrow diagram.
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Figure 20-24bX-Ray structure of the Ca2ATPase
from rabbit muscle sarcoplasmic reticulum. (b) A
schematic diagram of the structure viewed
similarly to Part a.
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Figure 20-32 Composite model of the KV channel.
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