Cell Biology
Exam Materials
Course Introduction
Cell Biology is a foundational course that explores the structure, function, and dynamics of cells, the basic units of life. The course covers key topics such as cell theory, cellular organelles, membrane structure and transport, energy production, cell signaling, genetic information flow, and cell division. Students will investigate how cells interact with their environment, maintain homeostasis, and give rise to complex tissues and organisms. Emphasis is placed on experimental techniques in cell biology, the molecular mechanisms underlying cellular processes, and the implications of cell biology in health and disease.
Recommended Textbook
Biochemistry 8th Edition by Jeremy M. Berg
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Page 2
Chapter 1: Biochemistry: An Evolving Science
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Q1) What gives proteins such a dominant role in biochemistry?
A) the rigidity of the peptide backbone
B) the ability to act as a blueprint
C) the ability to self-replicate
D) the ability to spontaneously fold into complex three-dimensional structures
E) All of the answers are correct.
Answer: D
Q2) Which of the following describes the relationship between the strengths of hydrogen and covalent bonds?
A) Hydrogen bonds are always stronger than covalent bonds.
B) Hydrogen bonds and covalent bonds have equivalent strength.
C) Hydrogen bonds are always weaker than covalent bonds.
D) With a few exceptions, most hydrogen bonds are stronger than covalent bonds.
E) With a few exceptions, most covalent bonds are stronger than hydrogen bonds.
Answer: C
Q3) How is water able to be a solvent for so many biological molecules?
Answer: Many biological molecules have polar characteristics.Water is extremely polar and is capable of competing with other polar molecules by weakening their electrostatic and hydrogen bonds.The oxygen atom can act as a hydrogen-bond acceptor,and the hydrogen can act as a donor.
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Chapter 2: Protein Composition and Structure
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Q1) Collagen contains _____________________,a modified amino acid.
Answer: hydroxyproline
Q2) _______________ is a fibrous protein and is the primary component of wool and hair.
Answer: \(\alpha\)-Keratin
Q3) What do the amino acids Tyr,Asn,and Thr have in common?
A) aromatic rings
B) negatively charged at pH 7.0
C) positively charged at pH 7.0
D) double bonds in side chains
E) polar
Answer: E
Q4) The term "quaternary" with respect to protein structure means
A) a repeating structure stabilized by intrachain hydrogen bonds.
B) the ability to form all four kinds of noncovalent bonds.
C) a multisubunit structure.
D) a linear sequence of four amino acids.
E) None of the answers is correct.
Answer: C
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Chapter 3: Exploring Proteins and Proteomes
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Q1) Protein databases
A) can identify proteins from small stretches of amino acid sequences.
B) are not useful in proteomics studies due to the complexities of the proteome.
C) are determined from sequence data only, never deduced from genomic data.
D) None of the answers is correct.
E) All of the answers are correct.
Answer: A
Q2) Which of the following affect the sedimentation rate of a particle?
A) mass
B) shape
C) the density of the solution
D) All of the answers are correct.
E) mass and shape
Answer: D
Q3) Molecular exclusion or gel-filtration chromatography separates molecules on the basis of __________________.
Answer: size
Q4) Proteins can be separated from small molecules and ions through a semipermeable membrane by __________________.
Answer: dialysis
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Chapter 4: DNA, RNA, and the Flow of Genetic Information
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Q1) The flow of genetic information from DNA to protein is called _____.
A) replication
B) transcription
C) translation
D) gene expression
E) All of the answers are correct.
Q2) A noncoding region within a gene is known as a _____.
A) intron
B) exon
C) missense region
D) split gene
E) None of the answers is correct.
Q3) What are two features of mature eukaryotic mRNA that are unique as compared to prokaryotic mRNA?
Q4) Stop codons are read by
A) initiation factors
B) transcription factors
C) release factors
D) elongation factors
E) None of the answers is correct.
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Chapter 5: Exploring Genes and Genomes
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Q1) The specificity or stringency of a PCR reaction can be controlled by altering the reaction
A) volume.
B) target sequence.
C) temperature and salt concentration.
D) time.
E) None of the answers is correct.
Q2) Briefly outline how a cDNA library is made.
Q3) Plasmids used in recombinant DNA technology typically
A) possess a gene for antibiotic resistance.
B) replicate independently of the host genome.
C) are circular double-stranded molecules.
D) contain reporter genes.
E) All of the answers are correct.
Q4) How is a gene gun used?
Q5) Bacterial plasmid DNA and bacteriophage DNA are commonly used ______________ to introduce foreign DNA into a bacterium.
Q6) A number of tools are critical to gene exploration.Name at least four.
Q7) The enzyme _________________ can be used to add nucleotides to the 3' end of DNA.
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Chapter 6: Exploring Evolution and Bioinformatics
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Q1) Which of the following would be classified as paralogs due to development of a new function from a duplication and subsequent mutation of a gene?
A) hemoglobin and myoglobin.
B) actin and keratin.
C) DNA polymerase and trypsin.
D) actin and myosin.
E) None of the answers is correct.
Q2) ___________________ can be detected in proteins by attempting to align a given sequence with itself,internally.
Q3) What evidence exists for a duplication event that led to the \(\alpha\) and \(\beta\)-hemoglobin?
Q4) What is the population of molecules in which it is easy to study evolutionary processes using combinatorial chemistry?
A) proteins
B) nucleotides
C) lipids
D) All of the answers are correct.
E) None of the answers is correct.
Q5) __________________ are homologous molecules that are found in a given species.
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Chapter 7: Hemoglobin: a Portrait of a Protein in Action
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Q1) Which of the following is the immediate product of the reaction between carbon dioxide and water?
A) HCO<sub>2</sub>H
B) HCO<sub>3</sub><sup>-</sup>
C) CO<sub>3</sub><sup>2</sup><sup>-</sup>
D) H<sub>2</sub>CO<sub>3</sub><sup>-</sup>
E) None of the answers is correct.
Q2) Carbon dioxide forms carbamate groups in proteins by reaction with A) aspartate residues.
B) cysteine residues.
C) N-terminal amino groups.
D) tyrosine residues.
E) heme groups.
Q3) The structure of normal adult hemoglobin can be described as a tetramer composed of
A) four myoglobin molecules.
B) two dimers.
C) two <sub>2</sub> and two <sub>2</sub> dimers.
D) two <sub>2</sub> and two <sub>2</sub> dimers.
E) None of these accurately describe hemoglobin.
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Chapter 8: Enzymes: Basic Concepts and Kinetics
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Q1) What is the Michaelis-Menten equation? Define all parameters.
Q2) In an enzymatic reaction in a test tube,the reaction will eventually reach equilibrium.Why does this not happen in living organisms?
Q3) When G for a system is zero,the system is at ______________________.
Q4) A(n)_____ requires an input of energy to proceed.
A) reaction at equilibrium
B) irreversible reaction
C) spontaneous reaction
D) exergonic reaction
E) endergonic reaction
Q5) Most known enzymes are proteins; however,some ___________ molecules have been shown to possess catalytic activity.
Q6) What term describes the substance that is bound by an enzyme and converted to product?
A) inhibitor
B) substrate
C) coenzyme
D) prosthetic group
E) cofactor
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Chapter 9: Catalytic Strategies
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Q1) The sequence 6 bp restriction cleavage site for EcoRV is GATXXX.What is the complete sequence of the double-stranded restriction site?
Q2) How is the bicarbonate formed when carbonic anhydrase is present?
Q3) Which of the following techniques allows investigators to test the role of individual amino acids in the determination of enzyme structure/function relationships even if the investigated amino acid is not present in the active site?
A) stopped-flow assay
B) use of mechanism based inactivators
C) use of methylating agents
D) site-directed mutagenesis
E) None of the answers is correct.
Q4) What metal ion is required by carbonic anhydrase for activity?
A) Zn<sup>2+</sup>
B) Mg<sup>2+</sup>
C) Cu<sup>2+</sup>
D) Fe<sup>2+</sup>
E) Ni<sup>2+</sup>
Q5) What is the common nucleophile found in cysteine,metallo-,and aspartyl proteases?
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Chapter 10: Regulatory Strategies
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Q1) Do allosteric enzymes follow traditional Michaelis-Menten kinetics? Draw a graph of rate relative to substrate concentration for ATCase and compare it to a Michaelis-Menten enzyme.
Q2) Blood serum analysis of ____________________________ isozymes is used in the diagnosis of a myocardial infarction.
Q3) The regulatory effects of substrates on allosteric enzymes are referred to as _______________ effects.
A) homotropic
B) heterotropic
C) allotropic
D) All of the answers are correct.
E) None of the answers is correct.
Q4) What term describes multiple forms of homologous enzymes found within an organism?
A) zymogens
B) holoenzymes
C) isoenzymes
D) consensus enzymes
E) None of the answers is correct.
Q5) How does cigarette smoking relate to elastase function?
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Chapter 11: Carbohydrates
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Q1) Sugars are commonly linked to which amino acid residues in glycoproteins?
A) tyrosine and asparagine
B) serine, threonine, and asparagine
C) serine, tyrosine, and asparagine
D) serine and glutamine
E) threonine and glutamine
Q2) The influenza virus recognizes _______________ (a carbohydrate)residues of glycoproteins present on cell surface.
Q3) How does a genetic mutation account for some of the different human blood types?
Q4) _______________ is a disaccharide composed of galactose and glucose joined by a -1,4 glycosidic bond.
Q5) What is the role of l-selectin when produced by an embryo?
Q6) When an open-chain aldose cyclizes into a ring,it forms a _______________.
Q7) The simplest carbohydrates are the 3-carbon molecules:
A) d- and l-glyceraldehyde.
B) dihydroxyacetone and d- and l-glyceraldehyde.
C) dihydroxyacetone and glycerate.
D) dihydroxyacetone and glycerol
E) None of the answers is correct.
Q8) How is the d or l configuration determined?
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Chapter 12: Lipids and Cell Membranes
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Q1) Membranes are primarily comprised of
A) lipids.
B) proteins.
C) carbohydrates.
D) All of the answers are correct.
E) A and B.
Q2) What substance inhibits prostaglandin H<sub>2</sub> synthase-1 by blocking the channel through which the substrate,arachidonate,travels?
A) acetaminophen
B) Celebrex
C) ibuprofen
D) Vioxx
E) acetylsalicylic acid
Q3) How many molecules thick are membranes?
A) one
B) two
C) infinite
D) varying thickness, depending on structure
E) None of the answers is correct.
Q4) Ionized fatty acids readily form ______________ in aqueous solutions.
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Chapter 13: Membrane Channels and Pumps
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Q1) A P-glycoprotein transporter is also referred to as MDR protein,which is an acronym for _________________________.
Q2) Describe the acetylcholine receptor shape.
Q3) How does the potassium channel maintain selectivity for potassium versus sodium ions?
A) The ion size is the determining factor.
B) The size of the ion and associated waters relative to the pore size are the determining factors in channel selectivity.
C) Dehydration of the potassium ion is compensated energetically by interactions with oxygen atoms in the selectivity filter, which is not possible with sodium ions.
D) Potassium ions associate with six molecules of water while sodium associates with four, thus allowing selectivity.
E) None of the answers is correct.
Q4) Explain how a voltage-gated channel opens.
Q5) Tetrodotoxin,isolated from puffer fish,binds tightly and specifically to ___________ channels in nerve cells.
Q6) Why is it dangerous to eat puffer fish that are not properly prepared?
Q7) What is simple diffusion? Provide an example.
Page 15
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Chapter 14: Signal-Transduction Pathways
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Q1) Important second messengers include cAMP,cGMP,calcium ion,_______________________,and diacylglycerol.
Q2) The binding of IP<sub>3</sub> to the IP<sub>3</sub> receptor results in the release of __________ from the endoplasmic reticulum.
Q3) What is a disadvantage of using common molecules for signaling paths?
Q4) What enzyme becomes active when bound to Ca<sup>2+</sup> and diacylglycerol?
A) calmodulin
B) protein kinase A
C) protein kinase C
D) phospholipase C
E) adenylate cyclase
Q5) How does the binding of epinephrine to its receptor set a response in action?
A) It causes an exchange of GTP for G protein bound GDP.
B) It causes a pore to open, allowing proton/ion exchange.
C) It causes the release of insulin.
D) It causes G proteins to produce cGMP.
E) None of the answers is correct.
Q6) _______________________ binds to the extracellular side of -adrenergic receptors.
Q7) What happens when signaling paths are not terminated properly?
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Chapter 15: Metabolism: Basic Concepts and Design
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Q1) What is an activated carrier? Provide two examples.
Q2) What type of pathway can be either anabolic or catabolic depending on the energy conditions of the cell?
A) amphipathic
B) amphiprotic
C) amphibolic
D) amphoteric
E) None of the answers is correct.
Q3) What vitamin is used to make the electron carrier NADH?
A) riboflavin
B) niacin
C) folate
D) biotin
E) thiamine
Q4) Metabolic processes are regulated by
A) transcriptional regulation of the amount of enzyme.
B) allosteric control of enzyme activity.
C) accessibility of substrates by compartmentalization.
D) covalent modification of enzymes
E) All of the answers are correct.
Page 17
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Chapter 16: Glycolysis and Gluconeogenesis
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Q1) In alcoholic fermentation,the decarboxylation of pyruvate requires a coenzyme that contains the vitamin ______________.
Q2) The Embden Meyerhof pathway is also known as _____.
A) pentose phosphate pathway
B) glycolysis
C) citric acid cycle
D) gluconeogenesis
E) None of the answers is correct.
Q3) Describe the two isoforms of lactate dehydrogenase.
Q4) Two primary raw materials for gluconeogenesis in the human liver are
A) galactose and sucrose.
B) acetate and oxaloacetate.
C) lactate and alanine.
D) fructose and alanine.
E) lactose and lactate.
Q5) How is glycolysis maintained under anaerobic conditions?
Q6) Both hexokinase and glucokinase phosphorylate glucose.The function of glucokinase is to phosphorylate glucose in liver cells as a means to regulate blood-sugar levels.Would you expect its K<sub>M</sub> to be higher or lower than hexokinase? Explain your answer.
Page 18
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Chapter 17: The Citric Acid Cycle
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Q1) What are the steps involved (in order)in the conversion of pyruvate to acetyl-CoA?
A) decarboxylation, oxidation, transfer to CoA
B) decarboxylation, transfer to CoA, oxidation
C) oxidation, decarboxylation, transfer to CoA
D) oxidation, transfer to CoA, decarboxylation
E) None of the answers is correct.
Q2) Why is the isomerization of citrate to isocitrate a necessary step of the citric acid cycle?
Q3) The glyoxylate cycle enables plants to survive using only A) pyruvate.
B) acetate.
C) oxaloacetate.
D) lactate.
E) None of the answers is correct.
Q4) The ____________ cycle is a process by which plants and some bacteria can convert two-carbon acetyl units into four-carbon units (succinate)for glucose synthesis,energy production,and biosynthesis.
Q5) What is the energy source that drives the condensation of oxaloacetate and acetyl CoA to produce citrate?
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Chapter 18: Oxidative Phosphorylation
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Q1) In the initial step of Complex I,two high-potential electrons are transferred from NADH to the ___________ prosthetic group of this complex.
Q2) What evidence demonstrated the ATP synthase has components that can actually rotate?
Q3) In prokaryotes the site of ATP-synthesizing machinery is
A) the mitochondrial matrix.
B) the outer cell wall.
C) the cytoplasmic membrane.
D) the nucleolus.
E) None of the answers is correct.
Q4) The transfer of a single electron to O<sub>2</sub> forms the reactive _______________ ion.
Q5) Explain why carbon monoxide is toxic.
Q6) What are uncoupling agents? Provide an example of when these might be useful.
Q7) In the malate-aspartate shuttle,how is oxaloacetate regenerated since there is no transporter for oxaloacetate across the inner membrane?
Q8) Cytochrome ________ is the only water-soluble cytochrome of the electron-transport chain.
Page 20
Q9) Cytochrome c oxidase contains two heme A groups and three ______________ ions.
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Chapter 19: The Light Reactions of Photosynthesis
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Q1) How do herbicides such as diuron or atrazine work?
Q2) The pathway of electron flow from H<sub>2</sub>O to NADP<sup>+</sup> in photosynthesis is referred to as
A) cooperative special pairs.
B) photorespiration.
C) the Z scheme of photosynthesis.
D) photophosphorylation.
E) None of the answers is correct.
Q3) What cofactor is required by plastocyanin for proper activity?
A) manganese
B) iron
C) copper
D) magnesium
E) zinc
Q4) In _______________,ATP is generated without the concomitant formation of NADPH.
Q5) Describe the process of cyclic photophosphorylation.
Q6) What are the likely reasons that manganese evolved as the ion used in photosystem II?
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Q7) After P960 absorbs light,what are the next few steps in bacterial photosynthesis?
Chapter 20: The Calvin Cycle and the Pentose Phosphate
Pathway
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Q1) A _______________ intermediate is formed between the carbonyl group of the ketose substrate and the -amino group of a lysine residue of transaldolase.
Q2) Give the sequence of reactions involved in the synthesis of sucrose from two glucose6-phosphate molecules.
Q3) Why is the chemistry of the "dark reactions" referred to as a cycle and not a pathway?
Q4) How can a deficiency of glucose 6-phosphate confer a physiological advantage?
Q5) Several physiological modes are possible for the metabolic need for NADPH,ribose 5-phosphate,and ATP.In one scenario,such as found in adipose tissue,much more NADPH is required than ribose 5-phosphate.How is this maintained?
Q6) The binding site of Mg<sup>2+</sup> to rubisco requires the formation of a ________________ group between lysine 201 and CO<sub>2</sub>.
Q7) Which form of thioredoxin activates certain Calvin cycle enzymes?
A) reduced
B) oxidized
C) dimeric
D) phosphorylated
E) dephosphorylated
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Chapter 21: Glycogen Metabolism
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Q1) Why must glycogen control be manifested differently in muscle and liver?
Q2) What are some of the advantages of having glycogen as a glucose source?
Q3) Why is the T state of glycogen phosphorylase less active?
A) The adjacent amino acids are not phosphorylated, and thus the catalysis cannot be carried out.
B) The active site is partially blocked.
C) ATP cannot be bound by the T state.
D) Glucose-1-phosphate remains bound to the active site.
E) None of the answers is correct.
Q4) Which of the following occur after a carbohydrate-rich meal?
A) Blood-glucose levels increase leading to glycogen storage in the liver.
B) Blood-glucose levels increase leading to glycogen storage in the muscle.
C) Glucose uptake from the blood increases as a result of the action of insulin.
D) Glucagon is absent.
E) All of the answers are correct.
Q5) ______________ markedly stimulates glycogen breakdown in muscle by initiating a cAMP signal-transduction cascade.
Q6) Insulin stimulates glycogen synthase by inactivating
Q7) How does insulin stimulate glycogen synthesis?
Q8) What are the fates of the glucose-1-phosphate derived from glycogen? Page 24
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Chapter 22: Fatty Acid Metabolism
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Q1) What is the approximate energy yield from complete oxidation of fatty acids?
A) 3 kcal g<sup>-1</sup>
B) 4 kcal g<sup>-1</sup>
C) 6 kcal g<sup>-1</sup>
D) 9 kcal g<sup>-1</sup>
E) 11 kcal g<sup>-1</sup>
Q2) What are four physiological roles for fatty acids?
Q3) Acetoacetate and ________________ are referred to as ketone bodies and are major fuel sources for heart muscle.
Q4) How are fatty acids larger than 16 carbons formed?
A) By elongation reactions catalyzed by enzymes on the endoplasmic reticulum
B) By one-carbon additions at the mitochondrial membrane
C) By elongation reactions catalyzed by enzymes in the peroxisomes
D) By addition of acetoacetyl CoA
E) None of the answers is correct.
Q5) What is the role of the acyl carrier protein in fatty acid synthesis?
Q6) The committed step of fatty acid synthesis is the formation of
Q7) \(\beta\) oxidation of odd-numbered fatty acids produces acetyl-CoA and
Q8) How is pyrophosphate formation an important theme in biochemistry? Page 26
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Chapter 23: Protein Turnover and Amino Acid Catabolism
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Q1) What class of enzymes cleaves most aromatic rings in biological systems?
A) dioxygenases
B) monooxygenases
C) biopterin-linked lyases
D) aromatic oxidases
E) None of the answers is correct.
Q2) What are some types of enzyme-catalyzed reactions that require pyridoxal phosphate as a coenzyme?
Q3) Surplus amino acids are
A) stored in proteosomes.
B) stored in protein scaffolds.
C) used as metabolic fuel.
D) stored as albumin.
E) None of the answers is correct.
Q4) Ketogenic amino acids are degraded to which of the following metabolites?
A) pyruvate
B) acetoacetate
C) oxaloacetate
D) \(\alpha\)-ketoglutarate
E) All of the answers are correct.
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Chapter 24: The Biosynthesis of Amino Acids
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Q1) At least _____________ ATP molecules are hydrolyzed for each N<sub>2</sub> reduced.
Q2) The enzyme _______________ contains a selenium analogue of cysteine.
Q3) Tyrosine is a precursor to the molecule(s)
A) melanin.
B) epinephrine.
C) serotonin.
D) melanin and epinephrine
E) melanin and serotonin.
Q4) The _______________ reaction establishes the stereochemistry at the -carbon atom in amino acids.
Q5) The ATP-binding region of the nitrogen-fixating reductase is a(n)___________ domain.
A) iron-sulfur
B) electron-binding
C) P-loop NTPase family
D) molybdenum-binding
E) All the answers are correct.
Q6) The -amino group found in most amino acids comes from _______________by a transamination reaction.
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Chapter 25: Nucleotide Biosynthesis
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Q1) The displacing nucleophile in pyrimidine synthesis is typically
A) ammonia or an amino group.
B) a metal ion.
C) coenzyme A.
D) pyridoxamine.
E) None of the answers is correct.
Q2) Hypoxanthine-guanine phosphoribosyltransferase catalyzes the formation of guanylate and _______________.
Q3) Which of the following is the final degradation product of purine catabolism?
A) xanthine
B) hypoxanthine
C) inosine
D) urate
E) None of the answers is correct.
Q4) The two nucleotides that can serve as energy currency in certain biomolecular paths are ATP and _______________.
Q5) What are advantages of high urate levels such as those found in higher primates (like humans)?
Q6) How is the reciprocal use of nucleotides useful in purine synthesis?
Q7) What reaction actually forms the six-member ring found in pyrimidines?
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Chapter 26: Biosynthesis of Membrane Lipids and Steroids
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Q1) ______________________ is the major carrier of cholesterol esters in the blood.
Q2) The synthesis of ____________________ is the committed step in cholesterol biosynthesis.
Q3) In mammalian cells,phosphatidate is synthesized in the outer mitochondrial membrane and the ____________________________.
Q4) Vitamin D<sub>3</sub> is converted into ______________________,which is an active hormone that functions as a transcription factor.
Q5) How is methionine metabolism related to the synthesis of phosphatidyl choline?
Q6) What metabolite is reduced to glycerol-3-phosphate for triacylglycerol synthesis?
A) glyceraldehyde-3-phosphate
B) 3-phosphoglycerate
C) phosphoenolpyruvate
D) dihydroxyacetone phosphate
E) None of the answers is correct.
Q7) A ___________________ is composed of a fatty acid linked to sphingosine via an amide bond.
Q8) What is phosphatidylcholine? How is it synthesized in mammals?
Q9) What are the steps in LDL uptake into cells?
Page 31
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Chapter 27: The Integration of Metabolism
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Q1) The primary function of aerobic glycolysis is to
A) degrade glucose to provide ATP.
B) provide carbon skeletons for biosynthesis.
C) provide NADH for lactate reduction.
D) provide NADPH for biosynthetic reactions
E) None of the answers is correct.
Q2) In a typical human male,which of the following most closely approximates the energy content (in kcal)of triacylglycerols stored in adipose tissue?
A) 13,500 kcal
B) 135,000 kcal
C) 1,350,000 kcal
D) 13,500 cal
E) None of the answers is correct.
Q3) What metabolic changes occur during the early fasting state?
Q4) Show how the metabolism of the liver and skeletal muscle is interconnected by blood glucose and alanine during strenuous exercise.
Q5) What is the cause of type 1 diabetes?
Q6) What are the plasma concentrations of glucose in the normal fasting and starvation states?
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Chapter 28: DNA Replication, repair, and Recombination
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Q1) Which of the following is (are)true?
A) Naturally occurring DNA usually has negative supercoiling.
B) Forms with the same linking number can be interconverted without cleavage.
C) The twist value rarely changes in naturally occurring DNA.
D) All the answers are correct.
E) Naturally occurring DNA usually has negative supercoiling, and forms with the same linking number can be interconverted without cleavage.
Q2) What type of topoisomerase does NOT require ATP?
A) type I
B) type II
C) type III
D) type IV
E) All topoisomerases require ATP.
Q3) What is a processive polymerase enzyme versus a distributive enzyme?
Q4) Why is shape complementarity so important in DNA replication?
Q5) One metal ion in the DNA polymerase reaction coordinates the 3'-hydroxyl group of the primer,and the second metal ion interacts with the ______________.
Q6) The tertiary structures in DNA are created by the process known as
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Chapter 29: RNA Synthesis and Processing
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Q1) 14.The template strand has the _______________ sequence as the RNA transcript (except T instead of U).
Q2) Name the three stages of RNA synthesis.
Q3) What is a common feature of both protein-dependent and protein-independent termination signals in transcription?
Q4) How does the antibiotic rifamycin function?
Q5) The first event in eukaryotic transcriptional activation is binding of
A) the TATA-box-binding protein (TBP) to the TATA box.
B) the SP-1 protein to the CAAT box.
C) the RNA polymerase 500 base pairs upstream of the CAAT and TATA boxes.
D) rho protein to DNA.
E) None of the answers is correct.
Q6) What complex is responsible for splicing mRNA precursors?
A) splicozyme
B) spliceosome
C) sRNA
D) splicicon
E) None of the answers is correct.
Q7) Approximately how many mRNA transcripts in higher eukaryotes undergo processing?
Q8) 18.The rho ( )protein terminates transcription by acting as a ________________. Page 34
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Chapter 30: Protein Synthesis
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Q1) What term describes the RNA-directed process of protein synthesis?
A) transcription
B) translation
C) Merrifield synthesis
D) ribozyme-directed protein synthesis
E) None of the answers is correct.
Q2) Initiation,elongation,and termination all require factors that are members of the ______________________ family.
Q3) Which of the following is (are)required for initiation of protein synthesis in bacteria?
A) mRNA
B) the 30S subunit
C) fmet-tRNA<sub>f</sub>
D) GTP
E) All of the answers are correct.
Q4) How does the size of an amino acid influence accurate attachment of the amino acid to the tRNA in aminoacyl-tRNA synthetase reactions?
Q5) Aminoacyl-tRNA synthetases contain both an activation site and a(n)__________________ site.
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Chapter 31: The Control of Gene Expression in Prokaryotes
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Q1) What type of chemical language allows prokaryotic cells to deduce population densities?
A) quorum sensing
B) colony collapse
C) satellite communication
D) biofilm sensing
E) None of the answers is correct.
Q2) What is the relationship between gene regulation and sequences in the genome?
Q3) A unit of gene expression that allows controlled and coordinated expression of a set of proteins is called a(n)__________________.
Q4) Is it likely that the DNA binding sites for a repressor evolved from a common ancestor?
Q5) The repressor protein promotes transcription of ________________ encoded by the virus when repressor levels are relatively low.
Q6) The twofold axis of symmetry of the lac repressor matches the symmetry of the
Q7) How does the Cro protein promote the lytic state?
Q8) Briefly explain how attenuation regulates transcription.
Q9) How was the interaction known as quorum sensing discovered?
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Chapter 32: The Control of Gene Expression in Eukaryotes
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Q1) Histone binding and wrapping of DNA reduces the DNA length by A) 2-fold.
B) 7-fold.
C) 20-fold.
D) 100-fold.
E) 1000-fold.
Q2) The technique ______________________ has been used to show that in eukaryotes,chromatin structure blocks a large number of potential protein binding sites.
Q3) When a steroid hormone receptor binds its ligand,it induces a conformational change in the ligand-binding domain which allows the binding of a(n)_______________.
Q4) What is a hypersensitive site in eukaryotic DNA?
Q5) Give examples of epigenomic changes resulting in different cell types.
Q6) The ______________ histone seals off the nucleosome at the location at which the linker DNA enters and leaves.
Q7) Seventy percent of the cytosines in human DNA are modified by methylation specifically in _______________ sequences.
Q8) Describe the functions of the two domains of a typical eukaryotic transcription factor.
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Chapter 33: Sensory Systems
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Q1) The sense of vision is due to the absorption of light by _________________cells in the eye.
Q2) How were genes identified for bitter tastants?
A) A specific taste was genetically linked to a chromosome region and the DNA sequence examined for a sequence similar to 7TM receptors.
B) Knockout mice were used to determine the exact sequence.
C) A hybridization analysis of all genes expressed in taste buds with 7TM probes was obtained.
D) Protein purification and characterization of a family of proteins were conducted.
E) Taste tests were conducted with humans deficient in 7TM receptors.
Q3) What clues about signaling can be gained by studying the structural motifs of proteins,such as the ankyrin repeats found in NompC?
Q4) What is the immediate effect of a photon on the structure of 11-cis retinal?
A) The molecule is polarized.
B) The molecule is released from the protein rhodopsin.
C) The molecule is converted to the all-trans-retinal.
D) The molecule is converted from an aldehyde to an alcohol (retinol).
E) The structure is not changed but accepts electrons.
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Chapter 34: The Immune System
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Q1) What is the significance of the J region of the \(\kappa\) light-chain locus?
A) Multiple J sites contribute to antibody diversity.
B) It provides a unique joining site for J and V genes, which is always the same.
C) It provides numerous sites for linkage to the V genes.
D) A and B are both correct.
E) A and C are both correct.
Q2) ___________________ sequences are recognized by proteins RAG-1 and RAG-2 and facilitate cleavage and religation of DNA segments.
Q3) What are the two lines of defense in our immune system?
Q4) Which antibody can cause allergic reactions?
A) IgA
B) IgD
C) IgE
D) IgG
E) IgM
Q5) What are Toll-like receptors and what pathogens do they recognize?
Q6) Explain why the amino terminal immunoglobulin domains of the L and H chains have hypervariable sequences.
Q7) What are positive and negative selection of T-cell receptors?
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Chapter 35: Molecular Motors
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Q1) Binding of ATP causes ______________.
A) a decrease in kinesin affinity for microtubules
B) an increase in kinesin affinity for microtubules
C) no change in kinesin affinity for microtubules
D) cross-linking of kinesin to microtubules
E) kinesin to completely dissociate from microtubules
Q2) Microtubules are tracks for kinesins and _________________.
Q3) Which of the following is common to myosins,kinesins,and dyneins?
A) P-loop NTPase
B) S1 fragment
C) EF-hand domain
D) hexameric AAA ATPase
E) None of the answers is correct.
Q4) What is F-actin?
Q5) Myosin light chains are related to the _______________ family of proteins.
Q6) Bacterial flagella are polymers composed of 53-kd subunits of a protein called _______________.
Q7) Briefly describe the structure of myosin.
Page 41
Q8) Single molecules of myosin in action were studied using __________________.
Q9) How do molecular motors work?
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Chapter 36: Drug Development
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Q1) Thiopurines such as 6-thioguanine are used to treat immune disorders and leukemia.Some individuals who are treated show signs of toxicity at doses well tolerated by most patients.Explain the reason for this toxicity.
Q2) Who is credited with the discovery of penicillin?
A) Louis Pasteur
B) Alexander Fleming
C) Selman Waksman
D) Paul Ehrlich
E) Gerhard Domagk
Q3) __________________ is an abundant protein that binds to and transports drugs everywhere the bloodstream flows.
Q4) Briefly explain why a drug candidate that has a partition coefficient (log P)greater than 5 is not a good candidate for oral bioavailability.
Q5) Give an example of how a drug was discovered by a chance observation.
Q6) Briefly describe the factors that will determine the concentration of a drug at the target site in the body.
Q7) A drug's concentration at its target site is affected by its ADME,which is an acronym that stands for
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