Download Bio 201, Fall 2010 Test 3 Study Guide Questions to be able to

Bio 201, Fall 2010
Test 3 Study Guide
Questions to be able to answer
1. What are the two ways that cells can interact with one another? Why is this important for
multicellular organisms?
2. For the following physical cell interactions, a) what type of cells b) what is the function
and c) what are the molecules involved?: Middle lamella, extracellular matrix, tight
junctions, desmosomes, plasmodesmata, gap junctions.
3. What is pectin, what are its chemical properties and how do they contribute to the
function of the middle lamella?
4. Why are there cations in the middle lamella?
5. Why do fruits and vegetables get mushy?
6. What is the series of connections between the molecules involved in the extracellular
matrix?
7. What do scurvy and muscular dystrophy have to do with the extracellular matrix?
8. Why are tight junctions important for membrane-bound proteins in the plasma
membrane?
9. How are desmosomes different from tight junctions?
10. Differentiate between plasma membrane use in plasmosdesmata and gap junctions.
11. Where are gap junctions found, and why is it important that calcium and cAMP are small
enough to pass through gap junctions?
12. What is the purpose of chemical communication between cells?
13. What are the steps in signal transduction?
14. What things make receptors bind to specific ligands?
15. What kinds of conditions result in high and low ligand/receptor affinity?
16. What is the dissociation constant? As the dissociation constant increases, what happens
to affinity?
17. Differentiate between desensitization, downregulation, and drug tolerance.
18. For intracellular receptors, where is the receptor found, are the ligands hydrophobic or
hydrophilic, how does the signal affect gene expression?
19. For G-protein linked receptors, where is the receptor found, are the ligands hydrophobic
or hydrophilic, name the steps in the process of signal transduction. Be sure to include
information about second messengers.
20. For tyrosine kinase receptor, are ligands hydrophilic or hydrophobic, in the example he
gave what do they have to do with the immune system, how does the receptor change,
how does it ultimately affect gene expression?
21. How do energy and stability relate to one another?
22. Where is energy stored in organisms?
23. What is a kilocalorie?
Bio 201, Fall 2010
24. What are the ΔGs for the catalysis of ATP, anabolysis of ADP, oxidation of glucose, and
oxidation of NADH?
25. How do we get ATP to react?
26. What are the five characteristics of enzymes?
27. What do enzymes do to allow biological reactions to proceed?
28. How do enzymes speed up reactions?
29. How do we regulate enzyme activity?
30. Describe the structure of ATP.
31. Why is ATP so energy rich?
32. How do cells use ATP to drive endergonic reactions?
33. How do we make energy-rich ATP?
34. Why is glucose broken down in lots of small steps?
35. How do cells reap the energy from breaking down glucose?
36. When glucose is oxidized, what is reduced?
37. Is glycolysis efficient?
38. Does glycolysis occur differently when there is oxygen present?
39. What are the steps in glycolysis?
40. What are the things put into glycolysis, and what things come out?
Vocabulary
Tissue, organ, middle lamella, pectin, extracellular matrix, collagen, cell cortex, integrins,
scurvy, muscular dystrophy, dystrophin, tight junctions, desmosome, plasmodesmata, gap
junctions, connexin, ligand, signal transduction, signal transduction cascade, ligand/receptor
affinity, dissociation constant, desensitization, downregulation, drug tolerance, intracellular
receptors, G-protein linked receptors, allosteric, GTP/GDP, adenylate cyclase, cAMP,
inhibitor, protein kinase A/C, phopholipase C, inositol tri-phosphate, tyrosine kinase
receptor, B cell, T cell, interleukin, receptor clustering, cross phosphorylation, signal
transducer and activator of transcription, antibody, metabolism, exergonic, endergonic,
catabolic, anabolic, kilocalorie, ATP/ADP, ΔG, activation energy, enzyme, catalytic/active
site, allosteric site, substrate, competitive inhibition, phosphoanyhydride bond, resonance
stabilization, coupled reaction, redox reaction, oxidation, reduction, cellular respiration,
glycolysis, anaerobic, kinase, phosphofructokinase, dehydrogenase, isomerase, pyruvate