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2011 BIOLOGY 1A03: CELLULAR & MOLECULAR BIOLOGY

DR. KAJIURA' S STUDY QUESTIONS for the TEST #1 CHAPTERS 3, 4, 5, 6, 7 & Related Lectures
These Study Questions reflect some of the importanttopicsdiscussedinDr.Kajiuraslectures and may identify topics mentioned in your textbook requiring further study. Although these study questions do not cover every topic discussed in the textbook or in lectures, they will assist you in preparing for TEST 1 (Thursday, Oct 20th). TEST #1 will evaluate lecture material, textbook information, "in-lecture" discussions, online postings, supplementary figures, and resources. Students should answer these questions well in advance of test. Answers to these study questions are found in your lecture notes, the lecture outlines, supplementary online information and figures, and in your textbook.

CHAPTER 3: PROTEIN STRUCTURE AND FUNCTION & RELATED LECTURES

1. a) Describe Stanley Millersspark-discharge experiment. b)DiscussthereasonswhyMillersresultsaresignificanttotheunderstandingofchemicalevolution. 2. What are some of the alternative hypotheses regarding chemical evolution? 3. What did the analysis of the Murchison meteorite suggest with regards to chemical evolution? 4.Definethetermsmonomerandpolymer. 5. a) Draw a diagram displaying the general condensation (dehydration) reaction between two amino acids. b) What type of the bond links between the two amino acids? Show how the bond is formed and the products. 6. In lectures, we reviewed that there are 20 major amino acids in living organisms. List the three main categories of amino acids. 7. Differentiate between three types of isomers and provide an example of each. 8. In lectures, we discussed that molecular structure (shape or the arrangement of side groups) is a key factor influencing function. Discuss this concept with regards to the examples of the different types of DOPA (Dihydroxy Phenyl-Alanine)asrelatedtothetreatmentofParkinsonsdisease. 9. An amino acid has atoms or functional groups, linked to a central carbon atom. List the groups or atoms of an amino acid. Show the groups attached to the alpha carbon of phenylalanine. 10. List and elaborate upon the four levels of protein structure: primary, secondary, tertiary, and quaternary. 11. What is the difference between the normal condition and the sickle cell condition with regards to the primary level of protein structure?

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12. State an example of a 4 structure protein. 13. What is the function of chaperone proteins (or chaperonins)? 14. What are prions and why are they significant? 15. Discuss the significance of optical isomers with regards to the thalidomide tragedy.

CHAPTER 4: NUCLEIC ACIDS AND THE RNA WORLD & RELATED LECTURES
1. Draw a diagram of the general structure a nucleotide, and clearly label each of the components. 2. How can the structural formulas of pyrimidines and purines be distinguished from one another? 3. Draw a clearly labeled diagram of the formation of a phosphodiester linkage. Display how the two monomers are linked and the products. 4. Describe the structure of the double helix. 5. Explain and elaborate upon how the double helix structure facilitates the copying of DNA. 6. Describe the technique of gel electrophoresis. Why is this technique useful for biologists?

CHAPTER 5: AN INTRODUCTION TO CARBOHYDRATES & RELATED LECTURES

1. List some of the major functions of carbohydrates. 2. Show how ring formation occurs in glucose. Draw the ring structures and differentiate between the and forms. 3. Distinguish between the terms monosaccharide, disaccharide, and polysaccharides. 4. Draw a diagram of the glycosidic linkage in maltose. Clearly label the linkage and show the monomers that joined to form maltose. 5. Name the specific linkages joining the monomers in starch, glycogen, cellulose, chitin, and peptidoglycan. 6. Name examples of polymers in which the following sugars are present: ribose, deoxyribose, glucose, and galactose. 7. Describe the structure of a branch point in glycogen and label the linkages. 8. Distinguish between the following conditions: lactose intolerance and galactosemia. Describe the symptoms of each of these conditions.

3 CHAPTER 6: LIPIDS, MEMBRANES, AND THE FIRST CELLS & RELATED LECTURES
1. State an important difference between the lipids and the other major groups of macromolecules in terms of the number of monomers and how they are linked, and their interaction with water. 2. List the main types of lipids and describe their functions. 3. a) Draw a glycerol molecule. b) A fatty acid becomes covalently bonded to glycerol. Show the bond or linkage structure. Name the type of reaction involved in this process and state the specific linkage formed. 4. Indicate the carbon numbers of four common fatty acids. Specify which are saturated and unsaturated. Also describe how this may be indicated in their molecular formulas. 5. List the molecules that may combine to form a triacylglyceride. 6. List the molecules of the hydrophobic tail and hydrophilic head of a phospholipid. 7. List the three main types of transport across membranes. 8. Explain how osmosis is different from simple diffusion. 9. Explain how simple diffusion is different from facilitated diffusion. 10. Differentiate between a hypertonic solution and a hypotonic solution. 11. Distinguish between the Davson-Danielli Sandwich model and the Singer-Nicholson Fluid Mosaic model. Why is the Davson-Danielli model considered incorrect and the Fluid Mosaic model currently accepted as a correct model of membrane structure. 12.Howdoesmembranecompositioninfluencemembranefluidity?Comparetheviscousstateandthefluid state. 13. Describe the freeze-fracture technique. 14. Describe the molecular basis of the condition, Cystic Fibrosis. What are the symptoms of individuals with Cystic Fibrosis.

CHAPTER 7: INSIDE THE CELL & RELATED LECTURES

1. Distinguish between prokaryotic cells and eukaryotic cells. 2. Describe the structures and functions of the nucleus, the nuclear envelope, chromatin, and the nuclear pore complex. 3. Describe the molecules, which are involved in the importation and exportation of proteins through the nuclear pores. 4. State the functions of rough ER and smooth ER. 5. Describe the movement of secretory proteins through the endomembrane system (5 steps). 6. Autophagy and phagocytosis occur within the cytoplasm, state the organelle involved and its activities.

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7. Differentiate between peroxisomes and vacuoles. 8. Describe a transport vesicle (origins & functions). 9. List the three main components of the cytoskeleton and the types of protein subunits from which they are made. 10. List the main functions of actin molecules and microtubules. 11. Explain how protein conformational change, use of ATP, and "walking" or "sliding" of microtubule doublets are interrelated. 12. Describe the arrangement of microtubules in a cilium, a basal body, and a centriole. 13. List and describe three examples of motility that depend upon microfilaments. 14. Describe the experiment which helped researchers determine the location of the NLS (nuclear localization signal). THIS INFORMATION IS COPYRIGHT MATERIAL (INTELLECTUAL AND ACADEMIC PROPERTY) OF DR. L. KAJIURA, DEPARTMENT OF BIOLOGY, MCMASTER UNIVERSITY. IT MAY BE USED ONLY FOR STUDY PURPOSES AND ONLY BY STUDENTS ENROLLED IN FALL 2011 BIOLOGY 1A03 (CELLULAR & MOLECULAR BIOLOGY). THIS INFORMATION MAY NOT BE REPRODUCED FOR ANY OTHER PURPOSE, NOR DISTRIBUTED TO ANY PERSON (USING ANY TYPE OF MEDIA), WHO IS NOT ENROLLED IN THE COURSE, EXCEPT BY WRITTEN PERMISSION OF THE BIOLOGY 1A03 PROFESSOR, DR. L. KAJIURA. COPYRIGHT 2011