Clinical Biochemistry
Chapter Exam Questions
Course Introduction
Clinical Biochemistry explores the chemical processes and substances that occur within the human body and their significance in health and disease. This course focuses on the principles and practices involved in analyzing biological fluids for the diagnosis, management, and monitoring of disease. Students learn about metabolic pathways, organ function tests, enzymology, acid-base balance, electrolyte disturbances, and the biochemical basis of diseases such as diabetes and cardiovascular disorders. Laboratory techniques, quality control, and interpretation of clinical data are emphasized to prepare students for practical application in clinical and research settings.
Recommended Textbook
Biochemistry 8th Edition by Jeremy M. Berg
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Chapter 1: Biochemistry: An Evolving Science
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Q1) Describe the shape of methane.
Answer: Methane is tetrahedral,with bond angles of about 109°.
Q2) The number of hydrogen bonds formed between A and T is _____.
A) 1
B) 2
C) 3
D) 4
E) 2 if in DNA, 3 if in RNA
Answer: B
Q3) The DNA backbone is made from repeating _____.
A) monosaccharide units
B) amino acid units
C) sugar-phosphate units
D) fatty acid
E) None of the answers is correct.
Answer: C
Q4) What is significant about the fact that metabolic processes are common to many organisms?
Answer: These metabolic processes are extremely old,geologically,originating in a common ancestor.
Page 3
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Chapter 2: Protein Composition and Structure
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Q1) Which amino acid forms disulfide bonds?
A) histidine
B) methionine
C) proline
D) serine
E) cysteine
Answer: E
Q2) What is the approximate mass of a protein containing 200 amino acids? (Assume there are no other protein modifications.)
A) 2,000
B) 11,000
C) 22,000
D) 222,000
E) None of the answers is correct.
Answer: C
Q3) What are prions?
Answer: Prions are proteins that can assume (after infection or by other causes)a new protein structure,which is self-propagating.Mammalian prion diseases are fatal.
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Chapter 3: Exploring Proteins and Proteomes
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Q1) Two-dimensional electrophoresis is a combination of what two techniques?
A) ion-exchange chromatography and affinity chromatography
B) ion-exchange chromatography and SDS-PAGE
C) SDS-PAGE and affinity chromatography
D) isoelectric focusing and SDS-PAGE
E) isoelectric focusing and ion-exchange chromatography
Answer: D
Q2) Briefly describe how an ELISA works.
Answer: In ELISA,the antigen of interest is complexed with a specific antibody under appropriate assay conditions,and excess antibody is removed.The antibody is complexed to an enzyme,which can be measured quantitatively using an appropriate substrate and assay tool,often by a colorimetric product formation.
Q3) _____ is the term to describe an original amino acid sequence for an uncleaved protein.
A) Apoprotein
B) Holoprotein
C) Nascent
D) Protomer
E) None of the answers is correct.
Answer: C
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Chapter 4: DNA, RNA, and the Flow of Genetic Information
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Q1) What is an advantage of codon degeneracy?
Q2) Although the right-handed double helix is the most well-known DNA structure,DNA can also form
A) triple strands.
B) straight chains.
C) branched chains.
D) left-handed helices.
E) All of the answers are correct.
Q3) In what type of organisms can genetic information flow from RNA to DNA?
A) bacteria
B) viruses
C) cyanobacteria
D) archaea
E) None of the answers is correct.
Q4) Who noted that A:T and G:C ratios in DNA are approximately 1:1?
A) James Watson
B) Rosalind Franklin
C) Erwin Chargaff
D) Francis Crick
E) None of the answers is correct.
Page 6
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Chapter 5: Exploring Genes and Genomes
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Q1) Genes can be inserted into eukaryotic cells by A) viruses.
B) plasmids.
C) microinjection.
D) All of the answers are correct.
E) None of the answers is correct.
Q2) The biological role of restriction enzymes in bacteria is to A) repair DNA.
B) induce DNA crossover.
C) cleave foreign DNA.
D) join gaps in DNA.
E) None of the answers is correct.
Q3) Which of the following DNA sequences contains a palindromic inverted repeat such as those recognized by restriction enzymes? (Note: Only one strand is shown.)
A) CAGTCC
B) GCATCC
C) CGATTAGC
D) GAGAGAGA
E) GCATATGC
Q4) Design a potential DNA-restriction enzyme site.Show both strands.
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Chapter 6: Exploring Evolution and Bioinformatics
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Q1) If using protein structure is a better method to determine evolutionary relationships,why is most analysis done using DNA sequences?
Q2) If a protein contains a repetitive region,what might be assumed,and what should be done next to test the hypothesis?
Q3) 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.
Q4) What are some of the inherent difficulties of using DNA from ancient samples?
Q5) What are the three criteria necessary for evolution to occur?
Q6) Evolutionary trees are constructed with the assumption that the number of sequence differences is related to the time since the two sequences
Q7) The process by which very different evolutionary pathways lead totwo proteins with similar functions is referred to as _________________ evolution.
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Chapter 7: Hemoglobin: a Portrait of a Protein in Action
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Q1) Describe how carbon dioxide affects the oxygenation of hemoglobin.
Q2) 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.
Q3) What is metmyoglobin?
Q4) Why is it advantageous for hemoglobin to have allosteric properties?
Q5) What condition results from a single point mutation of the hemoglobin \(\beta\) chain,producing the HbS variant?
A) \(\alpha\)-thalassemia
B) \(\beta\)-thalassemia
C) hemoglobin SC disease
D) hemolytic anemia
E) sickle-cell anemia
Q6) As the partial pressure of carbon dioxide increases,the affinity of oxygen binding to hemoglobin ______________.
Q7) Describe the concerted model to explain allosteric cooperative binding.
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Chapter 8: Enzymes: Basic Concepts and Kinetics
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Q1) Enzymes accelerate the rate of a chemical reaction by __________________ the activation energy of the reaction.
Q2) Organic cofactors are referred to as __________________.
Q3) There are six basic categories of enzymes.List the categories,and define the type of reaction.
Q4) What are transition-state analogs?
Q5) The K<sub>M</sub> is
A) equal to the product concentration at initial reaction conditions.
B) equal to the substrate concentration when the reaction rate is half its maximal value. C) proportional to the standard free energy.
D) All of the answers are correct.
E) None of the answers is correct.
Q6) Most known enzymes are proteins; however,some ___________ molecules have been shown to possess catalytic activity.
Q7) What does V<sub>max</sub> indicate?
Q8) A __________________ inhibitor often has a structure similar to the substrate and often reversibly binds to the active site of the enzyme but can be displaced by substrate.
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Chapter 9: Catalytic Strategies
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Q1) What modification is made to DNA that protects the host DNA from cleavage by host restriction endonucleases?
A) acetylation
B) methylation
C) phosphorylation
D) ubiquitination
E) adenylation
Q2) EcoRV cleaves cognate DNA with a specificity approximately _____ times that of non-cognate DNA.
A) 10
B) 1000
C) 10,000
D) 1,000,000
E) 100,000,000,000
Q3) In trypsin,the specificity pocket contains a/an ______________ residue that binds to the positive charge of the K or R residue of the substrate.
Q4) How is the bicarbonate formed when carbonic anhydrase is present?
Q5) Describe the secondary and tertiary structures in domains that form P-loops and bind phosphoryl groups.
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Chapter 10: Regulatory Strategies
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Q1) One type of hemophilia is due to A) vitamin K deficiency.
B) loss of the gene for prothrombin.
C) loss of the gene for antihemophilic factor.
D) All of the answers are correct.
E) None of the answers is correct.
Q2) Allosteric proteins
A) usually display hyperbolic Michaelis-Menten kinetics.
B) often display cooperativity.
C) always consist of several identical subunits.
D) usually display hyperbolic Michaelis-Menten kinetics and often display cooperativity.
E) All of the answers are correct.
Q3) What is the dual action of thrombin?
Q4) What term describes enzymes that are activated by proteolytic cleavage?
A) phosphatases
B) isozymes
C) kinases
D) zymogens
E) apoenzymes
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Chapter 11: Carbohydrates
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Q1) Which of the following is among the most abundant organic molecules in the biosphere?
A) glycogen
B) amylose
C) amylopectin
D) cellulose
E) chitin
Q2) Describe some of the functions of glycosaminoglycans and proteoglycans.
Q3) An aldehyde and alcohol can react to form a
A) hemialdol.
B) hemiketal.
C) hemiacetal.
D) All of the answers are correct.
E) None of the answers is correct.
Q4) A _______________ is a stereoisomer that is not a mirror image.
Q5) A given protein with several potential glycosylation sites can have many different glycosylated structures called ________________.
Q6) What is the role of mannose 6-phosphate? What disease is caused by lack of this terminal sugar on glycoproteins?
Page 13
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Chapter 12: Lipids and Cell Membranes
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Q1) ___________________ are aqueous compartments enclosed by a lipid bilayer which can be created in a laboratory.
Q2) In animals,________________ is the key regulator of membrane fluidity.
Q3) Which of the following membrane-bound organelles is thought to have evolved from bacteria by endosymbosis?
A) peroxisomes
B) mitochondria
C) cell walls
D) nuclei
E) endoplasmic reticulum
Q4) Membranes are primarily comprised of
A) lipids.
B) proteins.
C) carbohydrates.
D) All of the answers are correct.
E) A and B.
Q5) The temperature at which a phospholipid membrane transitions from a rigid to a fluid state is referred to as _______________.
Q6) Ionized fatty acids readily form ______________ in aqueous solutions.
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Chapter 13: Membrane Channels and Pumps
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Q1) What are the similarities between sodium,potassium,and calcium ion channels?
A) All allow passage of multiple different ions.
B) They contain homologous domains in the membrane spanning regions.
C) They all contain voltage-sensing segments that close the channel in response to a particular membrane potential.
D) They are capable of moving ions in both directions across a membrane.
E) None of the answers is correct.
Q2) ___________________ are an important class of channels that increase the rate at which water flows through membranes.
Q3) What is the "ball-and-chain" model?
Q4) What type of membrane transporter moves two species in opposite directions across a membrane?
A) symporter
B) antiporter
C) uniporter
D) cotransporter
E) None of the answers is correct.
Q5) Inorganic ions and most metabolites can flow between the interiors of cells joined by _______________.
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Chapter 14: Signal-Transduction Pathways
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Q1) How does binding of epinephrine initiate cAMP production? Discuss briefly in terms of receptor structure and function.
Q2) What is the primary messenger that is released by the adrenal gland?
A) dopamine
B) epinephrine
C) glucagon
D) insulin
E) acetylcholine
Q3) What is meant by an EF hand? Draw or describe the structure.
Q4) The enzyme responsible for induction of the phosphoinositide cascade is
A) phospholipase C.
B) phospholipase A.
C) C-dependent protein (CDP).
D) calmodulin.
E) None of the answers is correct.
Q5) The ________ receptor is approximately 50% identical in amino acid sequence with the EGF receptor and has similar domain structure,but it does not bind any known ligand.
Q6) How many 7TM membranes exist? What are some of their functions?
Q7) Protein kinase A phosphorylates serine and ___________ residues.
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Chapter 15: Metabolism: Basic Concepts and Design
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Q1) Reaction pathways that exclusively transform fuels into cellular energy are
A) anabolic.
B) catabolic.
C) allobolic.
D) amphibolic.
E) None of the answers is correct.
Q2) In vertebrate muscle,_________________ serves as a reservoir of high-potential phosphoryl groups that can be readily transferred to ADP to regenerate ATP.
Q3) In the second stage of catabolism,numerous small molecules are converted into _________________,a central molecule in metabolism.
Q4) Which of the following is the ultimate electron acceptor in aerobic organisms?
A) carbon dioxide
B) NAD<sup>+</sup>
C) FAD
D) oxygen
E) succinate
Q5) Which of the metabolic chemical reactions is most commonly used to break down foodstuffs?
Q6) What is the phosphorylation potential of a cell?
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Chapter 16: Glycolysis and Gluconeogenesis
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Q1) Which of the following are reasons that glucose is a common metabolic fuel used by living organisms?
A) In its stable ring structure, glucose is unlikely to nonezymatically glycosylate proteins.
B) It is one of the fuels formed under prebiotic conditions, thus available for primitive biochemical systems.
C) It is the only sugar used by the brain and kidney as a fuel source.
D) It is a ketose and thus a nonreducing sugar.
E) Both A and B are correct.
Q2) Which metabolic steps differ between glycolysis and gluconeogenesis?
Q3) What is substrate level phosphorylation?
A) phosphorylation of AMP by ATP
B) ATP synthesis when the phosphate donor is a substrate with high phosphoryl transfer potential
C) phosphorylation of glycolytic intermediates
D) phosphorylation of ATP coupled to an ion gradient
E) ATP and AMP synthesis from two molecules of ADP
Q4) A potent allosteric activator of liver phosphofructokinase is _____________________,which is produced from fructose-6-phosphate by PFK2.
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Chapter 17: The Citric Acid Cycle
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Q1) What is the enzyme-bound intermediate in the conversion of citrate and isocitrate?
A) oxalosuccinate
B) dihydrocitrate
C) cis-aconitate
D) hydroxyethyl-TPP
E) fumarate
Q2) What molecule initiates the citric acid cycle by reacting with oxaloacetate?
A) pyruvate
B) acetyl CoA
C) oxaloacetate
D) glucose
E) None of the answers is correct.
Q3) E2 of the pyruvate dehydrogenase complex contains a lipoyl group that is covalently attached to a _______________ residue of the enzyme.
Q4) Give the net equation of the citric acid cycle.
Q5) How is succinate dehydrogenase unique when compared to the other enzymes in the citric acid cycle?
Q6) How does the term "mad as a hatter" realistically reflect the condition?
Q7) Beri-beri is caused by a deficiency of __________________.
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Chapter 18: Oxidative Phosphorylation
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Q1) Which of the following does NOT participate in,nor is a component of,the electron-transport chain?
A) lipoic acid
B) nonheme, iron-sulfur proteins
C) FADH<sub>2</sub>
D) cytochrome c<sub>1</sub>
E) NADH
Q2) Provide a brief description of oxidative phosphorylation.
Q3) What type of gradient is critical to ATP formation by oxidative phosphorylation?
A) sodium ion
B) chloride ion
C) proton
D) potassium ion
E) None of the answers is correct.
Q4) In the malate-aspartate shuttle,how is oxaloacetate regenerated since there is no transporter for oxaloacetate across the inner membrane?
Q5) What is the driving force for electron transport through the electron-transport chain?
Q6) Discuss the evolution of the cytochrome c protein.
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Chapter 19: The Light Reactions of Photosynthesis
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Q1) In the light reactions of photosynthesis,the cooperation between photosystem II and photosystem I creates a flow of electrons from H<sub>2</sub>O to the final acceptor,_____________.
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 prosthetic group is associated with ferredoxin-NADP<sup>+</sup> reductase?
A) manganese center
B) plastoquinone
C) quinone A<sub>1</sub>
D) FAD
E) iron-sulfur center
Q4) The light-induced electron transfer in photosynthesis results in the transfer of ___________ into the thylakoid space.
Q5) What is the role of accessory pigments in photosynthesis?
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Chapter 20: The Calvin Cycle and the Pentose Phosphate
Pathway
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Q1) What intermediate is formed in the oxygenase reaction catalyzed by rubisco?
A) glyoxylate
B) hydroxypyruvate
C) glycerate
D) phosphoglycolate
E) malate
Q2) What prosthetic group is tightly bound to the enzyme transketolase?
A) biotin
B) tetrahydrofolate
C) FAD
D) pyridoxal phosphate
E) thiamine pyrophosphate
Q3) The C<sub>4</sub> pathway is necessary in tropical plants because A) at high temperatures, the plants cannot maintain sufficient water levels within the cells.
B) tropical plants do not have proper day/light cycles to maintain the balance of CO<sub>2</sub> necessary for carbohydrate storage.
C) at high temperatures, the oxygenase activity of rubisco is high.
D) All of the answers are correct.
E) None of the answers is correct.
Page 22
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Chapter 21: Glycogen Metabolism
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Q1) Which of the following serves as the glucose "sensor" enzyme in liver cells?
A) glucose-6-phosphatase
B) hexokinase
C) phosphoglucomutase
D) UDP-glucose pyrophosphorylase
E) phosphorylase a
Q2) Why is the formation of glucose-1-phosphate energetically favorable even though the G° is very small?
Q3) What molecule must be excluded from the active site of glycogen phosphorylase?
A) glucose
B) glucose 1-phosphate
C) water
D) phosphate
E) None of the answers is correct.
Q4) What path in addition to the cAMP-induced signal transduction is used in the liver to stimulate glycogen breakdown by epinephrine?
Q5) Why must glycogen control be manifested differently in muscle and liver?
Q6) Why can't the glucose 1-phosphate diffuse out of the cell?
Q7) What are the three steps in glycogen degradation?
23
Q8) Insulin stimulates glycogen synthase by inactivating
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Chapter 22: Fatty Acid Metabolism
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Q1) Acetyl-CoA carboxylase is inactivated when the energy charge of the cell is___________ (high,low).
Q2) How does fatty acid oxidation differ in peroxisomes?
A) The final product is not acetyl CoA but is succinyl CoA.
B) NAD<sup>+</sup> does not participate in the pathway.
C) The initial dehydrogenation reaction is different in that electrons are transferred to O<sub>2</sub> to yield H<sub>2</sub>O<sub>2</sub>.
D) All oxidations use NAD<sup>+</sup> as the oxidizing agent.
E) None of the answers is correct.
Q3) What pathway degrades an acyl-CoA into acetyl CoA?
A) acyl transferase cycle
B) chylomicron cycle
C) glyoxylate cycle
D) carnitine cycle
E) \(\beta\) oxidation
Q4) What are the similarities between fatty acid synthesis and degradation?
Q5) The synthesis of fatty acids takes place in the _____________ of the cell.
Q6) Calculate the amount of ATP generated from the total oxidation of an unactivated fatty acid with an acyl chain of 16 carbons.
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Chapter 23: Protein Turnover and Amino Acid Catabolism
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Q1) Write the net equation of the urea cycle and indicate whether energy is produced or consumed by the cycle.
Q2) Describe the glucose-alanine cycle and its significance in amino acid metabolism.
Q3) Uricotelic organisms release nitrogen as
A) NH<sub>4</sub><sup>+</sup>.
B) arginine.
C) uric acid.
D) urea.
E) None of the answers is correct.
Q4) 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.
Q5) Serine dehydratase catalyzes the conversion of serine into NH<sub>4</sub><sup>+</sup> and __________________.
Q6) What are some types of enzyme-catalyzed reactions that require pyridoxal phosphate as a coenzyme?
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Chapter 24: The Biosynthesis of Amino Acids
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Q1) In comparing transaminase enzymes,certain amino acids have been conserved.What are these amino acids,and how are they important in determining the proper chirality of the new amino acid?
Q2) The enzyme _______________ contains a selenium analogue of cysteine.
Q3) S-Adenosylmethionine carries _______________groups.
A) methyl
B) CO<sub>2</sub>
C) ammonia
D) formyl
E) None of the answers is correct.
Q4) Which of the following is a versatile carrier of several different one-carbon units?
A) pyridoxal phosphate
B) biotin
C) tetrahydrofolate
D) coenzyme A
E) None of the answers is correct.
Q5) The _______________ reaction establishes the stereochemistry at the -carbon atom in amino acids.
Q6) What is enzyme multiplicity?
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Chapter 25: Nucleotide Biosynthesis
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Q1) What is a general theme in purine ring synthesis,in terms of reaction logic and mechanism?
Q2) In ______________ biosynthesis,the base is assembled first and then attached to ribose.
Q3) What is/are the advantage or advantages of channeling intermediates by carbamoyl phosphate synthetase?
Q4) The committed step in purine nucleotide biosynthesis is the conversion of _______________ to phosphoribosylamine.
Q5) 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.
Q6) All of the nitrogen atoms found in nucleotides are ultimately derived from A) aspartate.
B) glutamine.
C) glycine.
D) asparagine.
E) aspartate and glutamine.
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Chapter 26: Biosynthesis of Membrane Lipids and Steroids
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Q1) Respiratory distress syndrome is caused by a failure in the biosynthetic pathway of A) sphingosine.
B) gangliosides.
C) dipalmitoyl phosphatidyl choline.
D) cholesterol.
E) bile salts.
Q2) What is the major site of triacylglycerol synthesis in mammals?
A) liver
B) adipose tissue
C) small intestine
D) kidney
E) pancreas
Q3) Phosphatidate is formed from
A) glycerol 3-phosphate and two fatty acyl CoA's.
B) glycerol and two free fatty acids.
C) pyruvate and triacylglycerol.
D) glycerol and two fatty acyl CoA's.
E) glycerol 3-phosphate and diacylglycerol.
Q4) How is methionine metabolism related to the synthesis of phosphatidyl choline?
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Chapter 27: The Integration of Metabolism
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Q1) ATP production from ___________________ is essential for long-distance running.
Q2) When running a marathon,fuel sources from ___________________,muscle,and adipose are used.
Q3) What are the plasma concentrations of glucose in the normal fasting and starvation states?
Q4) What fuel is used exclusively by muscles following a day of starvation?
A) glycogen
B) fatty acids
C) alanine
D) glucose
E) \(\beta\)-hydroxybutyrate
Q5) What are the two factors that have led to a propensity to gain weight in humans,and how can they be negated?
Q6) How do SOCS (suppressors of cytokine signaling)proteins inhibit receptor signaling? Give one example.
Q7) Obesity is defined as a BMI of greater than________________________.
Q8) What are some of the primary metabolic fates of acetyl CoA in animals?
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Q9) The microsomal ethanol-oxidizing system (MEOS)consumes oxygen and ______________,which leads to oxidative stress partly due to the inability to regenerate glutathione.
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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) How is the processivity of DNA polymerase III accomplished?
Q3) During prokaryotic DNA replication,the RNA primer pieces are removed by __________________.
Q4) The DNA strand that is replicated continuously is known as the
strand.
Q5) What describes the number of times a DNA strand winds around the helix axis when the axis lies in a plane?
A) linking number
B) writhe number
C) twist number
D) supercoil number
E) None of the answers is correct.
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Chapter 29: RNA Synthesis and Processing
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Q1) How does RNA polymerase find the proper binding site?
Q2) Which of the following changes the nucleotide sequence of RNA after transcription occurs,by processes other than RNA splicing?
A) RNA editing
B) RNA proofing
C) RNA substitution
D) RNA mutation
E) None of the answers is correct.
Q3) How does binding of heat-shock proteins differ between E.coli and Drosophila?
Q4) The role of GTP in self-splicing is
A) to provide energy.
B) a cofactor.
C) a necessary base for RNA editing.
D) an activator.
E) None of the answers is correct.
Q5) Describe some of the significant differences between eukaryotic and prokaryotic transcription and translation.
Q6) What is a common feature of both protein-dependent and protein-independent termination signals in transcription?
33
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Chapter 30: Protein Synthesis
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Q1) What are the names for the tRNA binding sites on the ribosome?
Q2) Class ____________ aminoacyl-tRNA synthetases acylate the 2 hydroxyl group of the terminal adenosine of tRNA.
Q3) What hypothesis explains why some tRNA molecules can bind to more than one codon?
A) jiggle hypothesis
B) shimmy hypothesis
C) teeter hypothesis
D) totter hypothesis
E) wobble hypothesis
Q4) What protein is toxic because it hydrolyzes a critical adenine base from the 28S rRNA molecule in eukaryotes?
A) chloramphenicol
B) ricin
C) puromycin
D) erythromycin
E) tetrodotoxin
Q5) Describe the subunits of E.coli ribosomes.
Q6) The activation of a tRNA involves the formation of a(n)__________________ intermediate.
Page 34
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Chapter 31: The Control of Gene Expression in Prokaryotes
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Q1) The repressor has the highest affinity for which of the DNA binding sites?
A) O<sub>R</sub>1
B) O<sub>R</sub>2
C) O<sub>R</sub>3
D) O<sub>R</sub>4
E) It has equal affinity for all sites.
Q2) How does the lac repressor inhibit transcription?
A) It binds to the RNA polymerase and prevents its association to the DNA.
B) It binds to the DNA and prevents the RNA polymerase from unwinding and transcribing the DNA.
C) It binds to RNA polymerase and causes a frame shift, thus producing an mRNA with a nonsense mutation.
D) It binds to the mRNA molecule, preventing ribosomes from binding.
E) None of the answers is correct.
Q3) What is a complex community of prokaryotes?
A) quorum
B) colony
C) satellite
D) leader colony
E) biofilm
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Chapter 32: The Control of Gene Expression in Eukaryotes
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Q1) A key reaction in gene repression is the deacetylation of these amino acids in histones.
A) serine
B) threonine
C) arginine
D) lysine
E) All the answers are correct.
Q2) Structural components of the nucleosome include A) transcription factors.
B) an octamer of core histones.
C) histone H8, which has an amino-terminal tail rich in leucine and isoleucine.
D) enhancer elements.
E) None of the answers is correct.
Q3) The repeating unit formed by the DNA wrapping around the histone core is called a(n)_________________.
Q4) Why must gene regulation be more complicated in eukaryotic cells when compared to prokaryotic cells?
Q5) A zinc finger domain is stabilized by a bound zinc ion through interactions with two __________ and two ______________ residues.
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Chapter 33: Sensory Systems
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Q1) Describe the steps leading to the detection of light.
Q2) Salty tastes are detected through _________________.
Q3) The _________________ family of receptors is involved in odor and some taste sensations.
Q4) What ion stimulates guanylate cyclase?
A) sodium
B) potassium
C) calcium
D) magnesium
E) hydrogen
Q5) Detection of touch includes several stimuli,and two of the key components include A) pressure and sharpness.
B) temperature and sound.
C) pressure and duration.
D) temperature and taste.
E) pressure and temperature.
Q6) What clues indicate that protein receptors are important in detection of smells?
Q7) How is sound converted to a biochemical signal?
Q8) What evidence is there that sweet receptors are heterodimeric?
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Chapter 34: The Immune System
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Q1) Does induced fit play a role in antigen:antibody binding?
Q2) T cells are made in the A) pancreas.
B) bone marrow.
C) thymus.
D) thalamus.
E) None of the answers is correct.
Q3) 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.
Q4) The CD4 protein is expressed by _______________cells.
Q5) The ___________________ is a common structure in IgG and other immune proteins that includes antiparallel strands in two sheets around a hydrophobic core.
Q6) Are unrelated humans likely to have similar class II genes?
Q7) Why is it difficult to develop a vaccine for AIDS?
Q8) How are pathogens inside cells destroyed by the immune system?
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Chapter 35: Molecular Motors
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Q1) How does the action of kinesin differ from that of myosin on its track?
Q2) During a muscle contraction,the thin filaments (actin,tropomyosin,troponin)slide along the _________________.
Q3) Briefly describe the structure of myosin.
Q4) What was learned using the optical trap laser studies?
Q5) Which of the following is a bundle of nine microtubule pairs surrounding two singlet microtubules?
A) axoneme
B) dynein
C) Arp-actin
D) tropomyosin
E) None of the answers is correct.
Q6) What is the cause of Charcot-Marie-Tooth disease?
Q7) Bacterial flagella rotate in one direction for smooth swimming and in the other direction to cause _______________.
Q8) Myosin light chains are related to the _______________ family of proteins.
Q9) Describe the experiment that supports the proposed role of the lever arm in myosin motor activity.
Page 39
Q10) How are flagellin subunits arranged in the bacterial flagellum?
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Chapter 36: Drug Development
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Q1) __________________ is an abundant protein that binds to and transports drugs everywhere the bloodstream flows.
Q2) Give three types of conjugation reactions that occur in the metabolism of xenobiotics.
Q3) In which phase of drug development do healthy volunteers take the drug for initial safety studies?
A) phase I trials
B) phase II trials
C) phase III trials
D) pre-clinical trials
E) None of the answers is correct.
Q4) How is genomic information used to develop new drugs?
Q5) Some bacteria are resistant to penicillin because they contain __________________ enzymes.
Q6) What term describes a molecule that binds to a target molecule?
A) substrate
B) effector
C) ligand
D) cosubstrate
E) None of the answers is correct.
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