Seminar Monday

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Seminar Monday Professor Mary Hatcher-Skeers
The Claremont Colleges-McKenna
"Structure and Dynamics in
DNA Binding Sites" Seminar 400 p.m. CB 485
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Figure 24-29 Segregation of PSI and PSII.
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Figure 24-30 Electron micrograph of thylakoids.
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Figure 24-31 The Calvin cycle.
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Figure 23-25 The pentose phosphate pathway.
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Figure 23-29 Mechanism of transketolase.
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Figure 23-30 Mechanism of transaldolase.
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Figure 23-31 Summary of carbon skeleton
rearrangements in the pentose phosphate pathway.
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Table 24-1 Standard and Physiological Free Energy
Changes for the Reactions of the Calvin Cycle.
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Figure 24-32 Algal 3BPG and RuBP levels on
removal of CO2.
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Figure 24-33a X-Ray structure of tobacco RuBP
carboxylase. (a) The quaternary structure of the
L8S8 protein.
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Figure 24-34 Probable reaction mechanism of the
carboxylation reaction catalyzed by RuBP
carboxylase.
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Figure 24-35 Light-activation mechanism of
FBPase and SBPase.
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Figure 24-36 Probable mechanism of the oxygenase
reaction catalyzed by RuBP carboxylaseoxygenase.
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Figure 24-37 Photorespiration.
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Figure 24-38 The C4 pathway.
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Chapter 25 Lipid MetabolismSuggested
problems 1, 4, 5, 6, 8, 9
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Table 25-1 Energy Content of Food Constituents.
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Figure 25-1 Mechanism of interfacial activation
of triacylglycerol lipase in complex with
procolipase.
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Figure 25-2 Catalytic action of phospholipase A2.
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Figure 25-3a Substrate binding to phospholipase
A2. (a) A hypothetical model of phospholipase A2
in complex with a micelle of lysophosphatidylethan
olamine.
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Figure 25-3b Substrate binding to phospholipase
A2.(b) Schematic diagram of a productive
interaction between phospholipase A2 and a
phospholipid contained in a micelle.
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Figure 25-4b Structure and mechanism of
phospholipase A2. (b) The catalytic mechanism of
phospholipase A2.
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Figure 25-6 Conversion of glycerol to the
glycolytic intermediate dihydroxyacetone
phosphate.
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Figure 25-7 X-Ray structure of human serum
albumin in complex with 7 molecules of palmitic
acid.
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Figure 25-8 Franz Knoops classic experiment
indicating that fatty acids are metabolically
oxidized at their b-carbon atom.
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Figure 25-9 Mechanism of fatty acid activation
catalyzed by acyl-CoA synthetase.
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Figure 25-10 Acylation of carnitine catalyzed by
carnitine palmitoyltransferase.
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Figure 25-11 Transport of fatty acids into the
mitochondrion.
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Figure 25-12 The ?-oxidation pathway of fatty
acyl-CoA.
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Figure 25-14 Metabolic conversions of hypoglycin
A to yield a product that inactivates acyl-CoA
dehydrogenase.
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Figure 25-15 Mechanism of action of
b-ketoacyl-CoA thiolase.
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Figure 25-16 Structures of two common unsaturated
fatty acids.
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Figure 25-17 Problems in the oxidation of
unsaturated fatty acids and their solutions.
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Figure 25-18 Conversion of propionyl-CoA to
succinyl-CoA.
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Figure 25-19 The propionyl-CoA carboxylase
reaction.
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Figure 25-20 The rearrangement catalyzed by
methylmalonyl-CoA mutase.
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Figure 25-21 Structure of 5-deoxyadenosyl-coba
lamin (coenzyme B12).
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Figure 25-23 Proposed mechanism of
methylmalonyl-CoA mutase.
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Figure 25-25 Ketogenesis the enzymatic
reactions forming acetoacetate from acetyl-CoA.
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Figure 25-28 A comparison of fatty acid ?
oxidation and fatty acid biosynthesis.
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Figure 25-29 The phosphopantetheine group in
acyl-carrier protein (ACP) and in CoA.
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Figure 25-30 Association of acetyl-CoA
carboxylase protomers.
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Figure 25-31 Reaction cycle for the biosynthesis
of fatty acids.
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Figure 25-32 The mechanism of carboncarbon
bond formation in fatty acid biosynthesis.
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