Course Introduction
Nutritional Biochemistry Exam Preparation Guide
Nutritional Biochemistry explores the molecular mechanisms by which nutrients, including carbohydrates, proteins, fats, vitamins, and minerals, are digested, absorbed, metabolized, and utilized within the human body. The course examines the biochemical pathways that regulate energy production, the synthesis and breakdown of biomolecules, and the interactions between diet and genetic expression. Emphasis is placed on understanding how nutrient imbalances and deficiencies can affect health at the cellular and systemic levels, as well as the role of nutrition in disease prevention and management.
Recommended Textbook
Biochemistry 8th Edition by Jeremy M. Berg
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Chapter 1: Biochemistry: An Evolving Science
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Q1) When solutions containing complementary single strands of DNA are mixed,a loss of entropy occurs.How is it that the Second Law of Thermodynamics is not violated?
Answer: Heat must be released to the surroundings.
Q2) What two properties of water are important for biological interactions?
A) the polarity of water
B) the density of water
C) the cohesive properties of water
D) the polarity of water and the cohesive properties of water
E) the density of water and the cohesive properties of water
Answer: D
Q3) What thermodynamic and free-energy changes participate in protein folding?
Answer: A combination of hydrogen bonds and van der Waals forces affect enthalpy and the entropy associated with hydrophobic interactions.
Q4) What is the significance of hydrogen bonding in biochemical structures such as DNA?
Answer: The bonds are weak enough to be easily disrupted; yet when many are present,they provide the stabilization necessary for larger structures such as DNA.
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Chapter 2: Protein Composition and Structure
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Q1) The configuration of most peptide bonds in a protein is _____.
A) cis
B) circular
C) parallel
D) trans
E) perpendicular
Answer: D
Q2) 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
Q3) Which amino acid side chains are capable of ionization?
Answer: The amino acids are Asp,Glu,His,Cys,Tyr,Lys,and Arg.
Q4) Why are all the theoretical combinations of phi and psi not possible?
Answer: Steric hindrances of the side chains make certain combinations and angles impossible.
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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) 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) How are monoclonal antibodies made?
Answer: They are made by fusion of an immortal myeloma cell line with a short-lived,antibody-producing cell.
Q4) Long proteins are often treated with the enzyme ______________,which cleaves the protein into smaller,easily analyzed peptides.
Answer: trypsin OR chymotrypsin OR thrombin
Page 5
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Chapter 4: DNA, RNA, and the Flow of Genetic Information
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Q1) What are the minimal components required for DNA replication?
Q2) Which of the following is correct concerning the adaptor molecule tRNA?
A) tRNA contains an anticodon sequence that serves as the template recognition site.
B) The amino acid is attached to the 5' end of tRNA.
C) tRNA contains a poly A tail at the 3' end.
D) tRNA is the largest RNA in the cell.
E) tRNA serves as the gene in some viruses.
Q3) Each three-base codon encodes a specific _____.
A) DNA nucleotide
B) mRNA nucleotide
C) tRNA nucleotide
D) rRNA nucleotide
E) amino acid
Q4) What advantage do phosphodiesters have compared to other esters?
Q5) Draw how the dNTP is added to a DNA strand at the 3' end.
Q6) What is DNA hybridization?
Q7) What is a consensus sequence?
Q8) What are the characteristics of Z-DNA and what does the Z in Z-DNA stand for?
Q9) How does RNA polymerase differ from DNA polymerase?
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Chapter 5: Exploring Genes and Genomes
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Q1) 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.
Q2) Complementary,single-strand overhangs that are produced by some restriction endonucleases are referred to as ___________________.
Q3) A plasmid is an example of a common ______.
A) cosmid
B) chromosome
C) gene
D) vector
E) None of the answers is correct.
Q4) The most common type of DNA sequencing is _____.
A) polymerase chain reaction method
B) Sanger dideoxy method
C) reverse transcriptase method
D) transformation method
E) restriction method
Page 7
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Chapter 6: Exploring Evolution and Bioinformatics
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Q1) Why are protein comparisons of three-dimensional shape more revealing than primary sequences?
Q2) Evolutionary trees provide relative scales of divergence.How can these be reconciled with real times?
A) by comparing the amount of sequence divergence
B) by comparing proteins from convergent evolution
C) by comparing proteins from both convergent and divergent evolution
D) by using fossil records when possible
E) None of the answers is correct.
Q3) Which of the following molecules is the most stable?
A) mRNA
B) hemoglobin
C) carbohydrates
D) rRNA
E) mitochondrial DNA
Q4) Evolutionary trees are constructed with the assumption that the number of sequence differences is related to the time since the two sequences
Q5) ___________________ can be detected in proteins by attempting to align a given sequence with itself,internally.
8
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Chapter 7: Hemoglobin: a Portrait of a Protein in Action
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Q1) Which is NOT correct concerning the accepted models that describe cooperative binding?
A) In the sequential model, the binding of a ligand changes the conformation of the subunit to which it binds, in turn inducing a change in neighboring subunits.
B) All known allosteric proteins exhibit either the concerted or sequential model exclusive of the other.
C) Both models incorporate a low affinity T-state and a higher affinity R-state.
D) Both models explain the sigmoid-shaped binding curve.
E) In the concerted model, all molecules exist either in the T-state or the R-state.
Q2) Describe the structure of normal adult hemoglobin.
Q3) What is the role of -hemoglobin stabilizing protein?
Q4) What functional role does the "distal histidine" play in the function of myoglobin and hemoglobin?
Q5) What is metmyoglobin?
Q6) Draw the oxygen-binding curve of myoglobin and that of hemoglobin.Indicate the partial pressure of oxygen in the lungs and the range of pressure in tissue.
Q7) What is fetal hemoglobin? How does it differ from adult hemoglobin?
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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) How is the substrate bound to the active site?
Q3) Examples of cofactors include
A) Zn<sup>2</sup><sup>+</sup>, Mg<sup>2</sup><sup>+</sup>, and Ni<sup>2</sup><sup>+</sup>.
B) biotin and thiamine pyrophosphate.
C) pyridoxal phosphate and coenzyme A.
D) biotin and thiamine pyrophosphate and pyridoxal phosphate and coenzyme A
E) All of the answers are correct.
Q4) The straight-line kinetic plot of 1/ V<sub>0</sub> versus 1/S is called a
Q5) Most known enzymes are proteins; however,some ___________ molecules have been shown to possess catalytic activity.
Q6) .Enzyme populations are studied with the use of ensemble methods.How would the data differ from a single-enzyme study?
Q7) 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.
Page 10
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Chapter 9: Catalytic Strategies
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Q1) What type of assay allows analysis of an enzyme catalyzed reaction in milliseconds?
A) multiple wavelength absorbance spectroscopy
B) fluorescence lifetime
C) stopped-flow
D) NMR
E) None of the answers is correct.
Q2) Which of the following is NOT a way in which enzymes stabilize a transition state?
A) causing the temperature of the environment to increase
B) covalent catalysis
C) using binding energy
D) general acid-base catalysis
E) catalysis by approximation
Q3) In proteases such as papain,a ___________________ residue is activated by hydrogen-bonding to a histidine residue.
Q4) Kinetic studies on myosins,in the presence and absence of divalent cations,show that ________________ is the true substrate for this enzyme.
Q5) What features of carbonic anhydrase allow the rapid hydration of carbon dioxide?
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Chapter 10: Regulatory Strategies
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Q1) Multifunctional kinases phosphorylate proteins by recognizing related sequences called
A) cAMP binding sequences.
B) calmodulin binding sequences.
C) pseudosubstrate sequences.
D) consensus sequences.
E) palindromes.
Q2) What term describes enzymes that are activated by proteolytic cleavage?
A) phosphatases
B) isozymes
C) kinases
D) zymogens
E) apoenzymes
Q3) What is the final step in the clotting pathway?
Q4) How can cleavage of a single peptide bond activate a zymogen?
Q5) Protein kinase A is activated by the binding of ________________ to specific sites on the regulatory subunit.
Q6) p-Hydroxymercuribenzoate displaces Zn<sup>2+</sup> from binding to crucial ______________ residues in ATCase.
Q7) Why might it have been surprising to find that CTP inhibits ATCase?
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Chapter 11: Carbohydrates
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Q1) What is the advantage of having different blood types within a species?
Q2) Glycoproteins are normally
A) found on membranes.
B) secreted as extracellular proteins.
C) found inside organelles.
D) All of the answers are correct.
E) found on membranes and secreted as extracellular proteins.
Q3) A _______________ is a five-membered ring formed from a monosaccharide.
Q4) Why is it more difficult to determine the structure of the oligosaccharides,when compared to amino acid sequences?
Q5) How is the d or l configuration determined?
Q6) The nutritional storage form(s)of glucose in plants is/are A) glycogen.
B) amylose.
C) amylopectin.
D) cellulose.
E) amylose and amylopectin.
Q7) Plant starch is composed of amylose,a linear polymer of glucose,and a branched polymer of glucose referred to as _______________.
Page 13
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Chapter 12: Lipids and Cell Membranes
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Q1) Explain the relationship between the endoplasmic reticulum and the nuclear membrane and one additional characteristic about the nuclear membrane that sets it apart from other membranes.
Q2) What term describes molecules that have both hydrophilic and hydrophobic moieties?
A) amphoteric
B) amphiprotic
C) amphibian
D) amphipathic
E) None of the answers is correct.
Q3) ___________________ are aqueous compartments enclosed by a lipid bilayer which can be created in a laboratory.
Q4) What are some molecules that form the polar head group of a phospholipid (bound to the phosphate)? Provide several examples.
Q5) __________________ contain a double bond three carbons from the distal end of the fatty acid.
Q6) What are the primary structural differences between phospholipids constructed from a glycerol platform and those from sphingosine?
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Chapter 13: Membrane Channels and Pumps
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Q1) Describe the proposed mechanism of the lactose permease symporter.
Q2) A channel that opens in response to binding a particular molecule is called a ________ channel.
A) passive diffusion
B) symport
C) ligand-gated
D) ABC-protein
E) None of the answers is correct.
Q3) Describe the functional domains of the sarcoplasmic reticulum Ca<sup>2+</sup> ATPase.
Q4) Why are gap junctions sealed when high concentrations of calcium ions and protons are present?
Q5) ___________________ are an important class of channels that increase the rate at which water flows through membranes.
Q6) The acetylcholine receptor is an example of a ____________-gated channel.
Q7) Membrane pumps ____________________(consume,produce,or transduce)energy.
Q8) Tetrodotoxin,isolated from puffer fish,binds tightly and specifically to ___________ channels in nerve cells.
Q9) Why is it dangerous to eat puffer fish that are not properly prepared? 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) Describe two roles of phosphatidylinositol 4,5-bisphosphate (PIP<sub>2</sub>)in signal transduction.
Q3) Examples of second messengers include A) cAMP.
B) calcium.
C) inositol 1,4,5-trisphosphate.
D) cGMP.
E) All of the answers are correct.
Q4) EGF signaling is terminated by the action of phosphatases and the hydrolysis of bound _____________ by Ras.
Q5) 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.
Q6) _______________________ binds to the extracellular side of -adrenergic receptors.
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Chapter 15: Metabolism: Basic Concepts and Design
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Q1) What is the phosphorylation potential of a cell?
Q2) Which of the following is the product from the complete oxidation of carbon-containing fuels under fully aerobic conditions?
A) oxygen
B) carbon monoxide
C) acetyl CoA
D) pyruvate
E) carbon dioxide
Q3) What is an activated carrier? Provide two examples.
Q4) What substance serves as the electron donor for most reductive biosynthetic pathways?
A) NADPH
B) NADH
C) FADH<sub>2</sub>
D) FMNH<sub>2</sub>
E) None of the answers is correct.
Q5) In the second stage of catabolism,numerous small molecules are converted into _________________,a central molecule in metabolism.
Q6) Why is ATP frequently bound to magnesium or manganese ions?
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Chapter 16: Glycolysis and Gluconeogenesis
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Q1) Describe the two isoforms of lactate dehydrogenase.
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) Which metabolic steps differ between glycolysis and gluconeogenesis?
Q4) What is the function of glyceraldehyde 3-phosphate dehydrogenase?
A) oxidation of an aldehyde by NAD<sup>+</sup> and formation of acyl-phosphate
B) oxidation of an alcohol to an aldehyde by NAD<sup>+</sup>
C) dehydration and dephosphorylation of GAP
D) hydrolysis of GAP
E) removal of the 3-phosphoryl-group from GAP
Q5) What two isomerization reactions occur in glycolysis? Why are these steps necessary?
Q6) How is the conversion of phosphoenolpyruvate to pyruvate accompanied by ATP formation?
Q7) In the absence of oxygen,_____________________ increases the expression of most glycolytic enzymes and the glucose transporters GLUT1 and GLUT3.
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Chapter 17: The Citric Acid Cycle
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Q1) In which reaction is GTP (or ATP)directly formed in the citric acid cycle?
A) conversion of succinyl CoA to succinate
B) decarboxylation of \(\alpha\)-ketoglutarate
C) conversion of isocitrate to \(\alpha\)-ketoglutarate
D) condensation of acetyl-CoA and oxaloacetate
E) None of the answers is correct.
Q2) Which of the following is toxic due to its ability to react with neighboring sulfhydryls of dihydrolipoyl groups,thus blocking their reoxidation to lipoamide?
A) fluoroacetate
B) carbon monoxide
C) arsenite
D) rotenone
E) cyanide
Q3) How does the decarboxylation of \(\alpha\)-ketoglutarate resemble that of pyruvate decarboxylation?
Q4) Why is it necessary that there be a mechanism to replenish oxaloacetate?
Q5) Explain why a GTP is energetically equivalent to an ATP in metabolism.
Q6) In the citric acid cycle,one __________ is produced by a substrate-level phosphorylation.
Page 20
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Chapter 18: Oxidative Phosphorylation
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Q1) Cytochrome c oxidase contains two heme A groups and three ______________ ions.
Q2) Electron flow down the electron-transport chain leads to the
A) transport of protons across the inner mitochondrial membrane from inside the matrix to the intermembrane space.
B) transport of protons across the inner mitochondrial membrane from the intermembrane space into the matrix.
C) coupled synthesis of GTP.
D) a dangerous imbalance of K<sup>+</sup> ions across the mitochondrial membrane.
E) None of the answers is correct.
Q3) Cytochrome ________ is the only water-soluble cytochrome of the electron-transport chain.
Q4) Which of the following does not pump protons?
A) Complex I
B) Complex II
C) Complex III
D) Complex IV
E) All of the answers are correct.
Q5) Explain why carbon monoxide is toxic.
Q6) How is oxidative phosphorylation regulated?
Page 21
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Chapter 19: The Light Reactions of Photosynthesis
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Q1) ______________________ is the term for a bacteriochlorophyll that has two protons instead of a magnesium ion at its center.
Q2) How is light used in photosynthesis?
A) The light is necessary to make the chlorophyll green, so the pigment can transmit electrons.
B) The light is used to generate high-energy electrons with great reducing potential.
C) The light provides heat energy for the chloroplasts.
D) The light is absorbed by oxygen which is converted into water.
E) None of the answers is correct.
Q3) What ion is found at the center of the tetrapyrole in chlorophyll a?
A) calcium
B) manganese
C) iron
D) copper
E) magnesium
Q4) P680 is the pigment reaction center for ____________________.
Q5) Describe the arrangement of the photosynthetic assemblies in the thylakoid membranes.
Q6) Describe the process of cyclic photophosphorylation.
Page 22
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Chapter 20: The Calvin Cycle and the Pentose Phosphate
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Q1) Which of the following is a readily mobilized sugar that is commonly used to transport carbohydrates through a plant?
A) glucose
B) fructose
C) sucrose
D) amylose
E) amylopectin
Q2) Give the sequence of reactions involved in the synthesis of sucrose from two glucose6-phosphate molecules.
Q3) Describe the three stages of the Calvin cycle.
Q4) Describe the role of thioredoxin in regulating the Calvin cycle.
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) How can a deficiency of glucose 6-phosphate confer a physiological advantage?
Q7) Why is the chemistry of the "dark reactions" referred to as a cycle and not a pathway?
Page 23
Q8) Which enzyme is cited as the most abundant enzyme in the biosphere? Why is this so?
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Chapter 21: Glycogen Metabolism
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Q1) The complete oxidation of a glucose residue from glycogen produces ________________ molecules of ATP in the muscle.
Q2) What protein serves as the primer for glycogen synthase?
A) branching enzyme
B) debranching enzyme
C) glycogenin
D) calmodulin
E) None of the answers is correct.
Q3) The glycogen branching enzyme moves a block of __________ (or so)glucose residues to form a branch point at least four residues from a preexisting branch.
Q4) What are the fates of the glucose-1-phosphate derived from glycogen?
Q5) What physiological conditions render phosphorylase b less active?
A) High ATP, AMP, and glucose 6-phosphate levels
B) High ATP and low calcium ion levels
C) High ATP and glucose 6-phosphate levels
D) High AMP and low ATP levels
E) None of the answers is correct.
Q6) In skeletal muscle,the binding of ___________ converts phosphorylase b into the active form.
Page 25
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Chapter 22: Fatty Acid Metabolism
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Q1) Describe the processes that dietary triacylglycerols must go through to be absorbed by intestines and transported in the blood stream.
Q2) The function of the enzyme acyl CoA synthetase is
A) lipolysis to release free glyceraldehyde.
B) ATP-dependent reduction prior to activation.
C) ATP-dependent activation of fatty acids using CoA.
D) Production of acetyl CoA for the TCA cycle
E) None of the answers is correct.
Q3) What tissue is the primary storage site for triacylglycerols in animals?
A) liver
B) adipose
C) kidney
D) heart
E) muscle
Q4) Why are triacylglycerols an excellent design for energy stores?
A) They are anhydrous.
B) They are small.
C) They are highly reduced.
D) They are anhydrous, and they are small.
E) They are anhydrous, and they are highly reduced.
Page 26
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Chapter 23: Protein Turnover and Amino Acid Catabolism
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Q1) Explain the cause of PKU,and give the structure of the abnormal metabolite that accumulates from which this condition gets its name.
Q2) Ubiquitin-tagged proteins are digested by the __________________.
Q3) In the first step of the urea cycle,CO<sub>2</sub> and NH<sub>4</sub><sup>+</sup> are converted into __________________.
Q4) Write the net equation of the urea cycle and indicate whether energy is produced or consumed by the cycle.
Q5) What molecule is formed from excess ammonium ions by ureotelic organisms?
A) uric acid
B) urea
C) ammonia
D) xanthine
E) hypoxanthine
Q6) Biopterin is a complicated coenzyme required for the conversion of Phe to Tyr.Why is biopterin not considered a vitamin?
Q7) The hydrolysis of arginine by arginase produces ornithine and ______________.
Q8) Describe the glucose-alanine cycle and its significance in amino acid metabolism.
Q9) What is the fate of sulfur in the metabolism of cysteine?
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Chapter 24: The Biosynthesis of Amino Acids
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Q1) What is enzyme multiplicity?
Q2) The -amino group found in most amino acids comes from _______________by a transamination reaction.
Q3) Which of the following is a vasodilator that is derived from histidine?
A) epinephrine
B) norepinephrine
C) histamine
D) adenosine
E) prostacyclin
Q4) Homocysteine is an intermediate in the synthesis of cysteine and _______________.
Q5) Amino acid synthesis is primarily regulated by A) turnover.
B) diet.
C) urea excretion.
D) allosteric enzyme regulation.
E) All the answers are correct.
Q6) What is the activated methyl cycle?
Q7) Describe the structure and function of the FeMo cofactor.
Q8) What is catalytic substrate channeling?
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Chapter 25: Nucleotide Biosynthesis
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Q1) Briefly describe,in one or two sentences,the reaction by which carbamoyl phosphate synthetase acquires an ammonia to make carbamoyl phosphate.
Q2) Dihydrofolate reductase is an excellent target for anticancer drugs because it is critical in the synthesis of _______________.
Q3) What is the intermediate in the conversion of inosinate to guanylate?
A) adenylate
B) cytidylate
C) guanylate
D) orotidylate
E) xanthylate
Q4) Why do purine-salvage pathways save the cell energy?
Q5) Which nucleotide is most commonly used as an energy currency?
A) ATP
B) UTP
C) GTP
D) CTP
E) TTP
Q6) The committed step in purine nucleotide biosynthesis is the conversion of _______________ to phosphoribosylamine.
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Chapter 26: Biosynthesis of Membrane Lipids and Steroids
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Q1) In mammalian cells,phosphatidate is synthesized in the outer mitochondrial membrane and the ____________________________.
Q2) What is phosphatidylcholine? How is it synthesized in mammals?
Q3) Which of the following vitamins is a derivative of cholesterol?
A) vitamin A
B) vitamin D
C) vitamin E
D) vitamin K
E) None of the answers is correct.
Q4) Which of the following metabolites is the source of all carbons for cholesterol?
A) glucose
B) pyruvate
C) succinyl CoA
D) oxaloacetate
E) acetyl CoA
Q5) In the biosynthesis of sphingosine,the condensation of palmitoyl CoA and serine requires the coenzyme ____________________.
Q6) What are the causes and symptoms of familial hypercholesterolemia?
Q7) How are gangliosides synthesized?
Page 30
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Chapter 27: The Integration of Metabolism
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Q1) ____________________ results when insulin is absent due to autoimmune destruction of the cells of the pancreas.
Q2) What are the three primary sources of glucose 6-phosphate in liver cells?
Q3) Show how the metabolism of the liver and skeletal muscle is interconnected by blood glucose and alanine during strenuous exercise.
Q4) What is the primary source of energy used by the muscle during starvation?
A) glucose
B) lactate
C) fatty acids
D) ketone bodies
E) branched-chain amino acids
Q5) Explain what is meant by the term the starved-fed cycle.What are the stages?
Q6) What is the key regulatory enzyme in glycolysis?
A) phosphofructokinase
B) glucokinase
C) hexokinase
D) triose phosphate isomerase
E) None of the answers is correct.
Q7) What is the advantage of converting pyruvate to lactate in skeletal muscle?
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Chapter 28: DNA Replication, repair, and Recombination
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Q1) 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.
Q2) What is true about DNA polymerases?
A) There are at least five structural classes.
B) All have finger and thumb domains that wrap around the DNA.
C) All catalyze the same reaction, which requires metal cofactors.
D) All the answers are correct.
E) There are five structural classes, and all catalyze the same reaction, which requires metal cofactors.
Q3) Describe the general three-step process that is catalyzed by a type I topoisomerase.
Q4) What is a Klenow fragment?
Q5) Describe the consequences of incorrect DNA replication or DNA damage.
Q6) The human genetic skin disease caused by a mutation in components of the human nucleotide-excision-repair pathway is called ___________________.
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Chapter 29: RNA Synthesis and Processing
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Q1) tRNA and rRNA modification in prokaryotes includes
A) cleavage and modification of nascent RNA.
B) addition of nucleotides.
C) spliceosome-mediated splicing of the nascent RNA.
D) All the answers are correct.
E) cleavage and modification of nascent RNA and addition of nucleotides.
Q2) 20.RNA self-splicing demonstrates the role of RNA as a __________________.
Q3) What is the definition of a promoter?
Q4) Which of the following is an RNA molecule that is catalytic?
A) tRNA
B) ribonuclease
C) ribozyme
D) RNA helicase
E) None of the answers is correct.
Q5) What term is used to describe the synthesis of RNA?
A) replication
B) splicing
C) translation
D) transcription
E) None of the answers is correct.
33
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Chapter 30: Protein Synthesis
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Q1) What sequence identifies a protein for translocation across the ER?
A) signal sequence
B) Shine-Dalgarno sequence
C) poly-A sequence
D) endoplasmic sequence
E) cargo sequence
Q2) Explain why some bases in some RNAs cannot be involved in base pairs.
Q3) What proteins recognize UAA,UAG,and UGA codons?
A) initiation factors
B) elongation factors
C) termination factors
D) release factors
E) 30s ribosome subunit
Q4) The ribosome is thought to be
A) an example of a catalyst that has survived from the RNA world.
B) unique to eukaryotes.
C) a ribozyme.
D) a protein catalyst.
E) an example of a catalyst that has survived from the RNA world and a ribozyme.
Q5) What is the function of yeast alanyl-tRNA?
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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 repressor promote the lysogenic state?
Q3) The twofold axis of symmetry of the lac repressor matches the symmetry of the
Q4) How do helix-turn-helix motifs interact with DNA?
Q5) What is a complex community of prokaryotes?
A) quorum
B) colony
C) satellite
D) leader colony
E) biofilm
Q6) In the helix-turn-helix motif of DNA binding proteins,the amino acid side chains of one helix bind to the __________________ and the other to the
Q7) 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) DNA regions that serve as binding sites for transcription factors which can act at a distance to perturb the local chromatin structure are called _________________.
Q2) 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.
Q3) 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.
Q4) 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)_______________.
Q5) Describe how the IRE-binding protein regulates ferritin levels when iron levels are low.
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Chapter 33: Sensory Systems
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Q1) What condition is characterized by the inability to smell certain compounds?
A) dysosmia
B) specific anosmia
C) ageusia
D) parosmia
E) Kallmann syndrome
Q2) Because the major clue to the mechanism of hearing is speed,sounds are detected through
A) 7TM receptors.
B) amiloride-sensitive ion channels.
C) chemical receptors.
D) mechanosensory ion channels.
E) None of the answers is correct.
Q3) 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.
Q4) What evidence is there that sweet receptors are heterodimeric?
Page 37
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Chapter 34: The Immune System
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Q1) The CD4 protein is expressed by _______________cells.
Q2) _______________ are molecules that induce differentiation,cell growth,and in certain cells,secretion of antibodies.
Q3) Proteins necessary for binding and displaying portions of foreign proteins are encoded by the ____________________.
Q4) How does the immune response differ for peptides bound to a class II,rather than class I,MHC protein?
Q5) What is the generic term used to denote what an antibody binds?
A) epitope
B) cytokine
C) affinity determinant
D) antigen
E) None of the answers is correct.
Q6) How is the immune system diversity similar to evolutionary processes?
Q7) The immunoglobulin with the highest serum concentration is _______________.
Q8) A(n)__________________ disease is one wherein the body attacks itself and produces self-antigens.
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Q9) When the heavy chain is switched to make secreted antibodies,how is the specificity of antigen binding maintained?
Chapter 35: Molecular Motors
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Q1) What are flagella used for in bacteria?
A) chemostasis
B) chemoselection
C) chemokinesis
D) chemotaxis
E) chemoprotection
Q2) During a muscle contraction,the thin filaments (actin,tropomyosin,troponin)slide along the _________________.
Q3) A helical section of myosin that moves dramatically when NTP is bound is called the ________.
Q4) What is the energy source used to rotate the flagella?
A) ATP
B) proton gradient
C) beta oxidation
D) GTP
E) None of the answers is correct.
Q5) What is the cause of Charcot-Marie-Tooth disease?
Q6) How is a bacterial motor similar to ATP synthase?
Q7) Briefly describe the structure of myosin.
Q8) Troponin reacts in response to the _______________ ion.
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Chapter 36: Drug Development
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Q1) Cyclooxygenase 2 is expressed primarily as part of the inflammatory response,whereas cyclooxygenase 1 is expressed more generally.Celecoxib (Celebrex)was designed to target COX2 and is used to reduce inflammation due to arthritis.What structural feature of Celecoxib (Celebrex)makes this drug more selective for COX2 instead of COX1?
Q2) Which of the following is conjugated to drugs to aid excretion?
A) glucuronic acid
B) cholic acid
C) glutamic acid
D) ascorbic acid
E) None of the answers is correct.
Q3) Which of the following properties affects the effective concentration of a drug at the target site?
A) the rate of absorption of the drug
B) the extent of distribution or compartmentalization of the drug
C) the efficiency of metabolism of the drug
D) the ease of excretion of the drug and/or its metabolites
E) All of the answers are correct.
Q4) How is genomic information used to develop new drugs?
Q5) Give an example of how a drug was discovered by a chance observation.
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