Biochemistry 7Th Ed By Berg Test Bank

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Biochemistry 7Th Ed By Berg Test Bank

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WITH ANSWERS
Biochemistry 7Th Ed By Berg Test Bank

Chapter 2   Protein Composition and Structure

 

 

Matching Questions

Use the following to answer questions 1-10:

 

Choose the correct answer from the list below. Not all of the answers will be used.

  1. a) l-amino acids
  2. b) water
  3. c) protons
  4. d) Zwitterions
  5. e) secondary structure
  6. f) tertiary structure
  7. g) Ramachandran
  8. h) cysteine
  9. i) extracellular
  10. j) histidine
  11. k) proline
  12. l) Sanger
  13. m) d-amino acids

 

1. ____________ Chiral type of amino acids found in proteins.

 

  Ans: a
  Section:  2.1

 

2. ____________ Another name for dipolar molecules.

 

  Ans: d
  Section:  2.1

 

3. ____________ Disulfide bonds are formed by pairs of which amino acid?

 

  Ans: h
  Section:  2.1

 

4. ____________ The amino acid with a pKa near neutral pH.

 

  Ans: j
  Section:  2.1

 

5. ____________ When a peptide bond is formed, what molecule is also made?

 

  Ans: b
  Section:  2.2

 

6. ____________ Where are proteins with extensive disulfide links likely to be found?

 

  Ans: i
  Section:  2.2

 

7. ____________ This amino acid residue frequently found in -turns.

 

  Ans: k
  Section:  2.1

 

 

8. ____________ Name of the plot that allows one to investigate the likely orientation of certain amino acid pairs.

 

  Ans: g
  Section:  2.2

 

9. ____________ The type of structure to which   helices, sheets, and turns are referred.

 

  Ans: e
  Section:  2.3

 

10. ____________ The overall three-dimensional structure of a protein is referred to as

 

  Ans: f
  Section:  2.4

 

 

Fill-in-the-Blank Questions

 

11. The amino acid that contains a sulfur atom and is consider hydrophobic  is _________________.
  Ans:  methionine     Section: 2.1

 

12. _______________ is a fibrous protein and is the primary component of wool and hair.
  Ans:  keratin     Section: 2.3

 

13. Every third residue in the protein collagen is ____________________.
  Ans:  glycine     Section: 2.3

 

14. Disulfide bonds in proteins can be reduced to free sulfhydryl groups by reagents such as _____________________.
  Ans:  mecaptoethanol     Section: 2.6

 

15. A protein is considered to be __________________ when it is converted into a randomly coiled structure without its normal activity.
  Ans:  denatured     Section: 2.6

 

16. ______________________ is the major fibrous protein present in skin, bone, tendon, cartilage, and teeth.
  Ans:  Collagen     Section: 2.3

 

17. Collagen contains _____________________, a modified amino acid.
  Ans:  hydroxyproline     Section: 2.6

 

18. Agents such as ______________________ and guanidine hydrochloride denature proteins by disrupting the noncovalent interactions.
  Ans:  urea     Section: 2.6

 

19. _____________________________ refers to the spatial arrangement of subunits and the nature of their interactions
  Ans:  Quaternary structure     Section: 2.5

 

20. The ________________________ -sheet structure occurs when the two strands are oriented in same directions (N C).
  Ans:  antiparallel     Section:  2.3

 

 

Multiple-Choice Questions

 

21. Proteins function as
  A) energy stores. D) None of the above.
  B) catalysts. E) All of the above.
  C) storage of genetic information.    
  Ans:  B     Section:  Introduction

 

22. Key properties of proteins include
  A) a wide range of functional groups.
  B) an ability to possess either rigid or flexible structures as dictated by functional requirements.
  C) the ability to interact with other proteins.
  D) a and b.
  E) All of the above.
  Ans:  E     Section:  Introduction

 

23. What charged group(s) are present in glycine at a pH of 7?
  A) NH3+     B) COO      C) NH2+     D) a and b     E) a, b, and c
  Ans:  D     Section:  2.1

 

24. At a pH of 12, what charged group(s) are present in glycine?
  A) -NH3+     B) -COO     C) -NH2+     D) a and b     E) a, b, and c
  Ans:  B     Section:  2.1

 

25. What do the amino acids tyr, asn and thr have in common?
  A) have aromatic rings D) contain double bonds in side chains
  B) are negatively charged at pH 7.0 E) are polar
  C) are positively charged at pH 7.0    
  Ans:  E     Section 2.1

 

26. Which amino acids contain a sulfur atom?
  A) serine and methionine D) cysteine and methionine
  B) serine and threonine E) cysteine and threonine
  C) methionine and threonine    
  Ans:  D     Section:  2.1

 

27. Name three amino acids that can be positively charged at a neutral pH.
  A) lys, arg, and his D) lys, arg, and pro
  B) his, arg, and cys E) arg, glu, and his
  C) cys, arg, and met    
  Ans:  A     Section:  2.1

 

28. In the following peptide, which amino acid is the N-terminus?

Phe-Ala-Gly-Arg

  A) Ala     B) Phe     C) Phe and Arg     D) Arg     E) None of the above.
  Ans:  B     Section:  2.2

 

29. What is the approximate mass of a protein containing 200 amino acids? (Assume there are no other protein modifications.)
  A) 20,000     B) 11,000     C) 22,000     D) 222,000     E) None of the above.
  Ans:  C     Section:  2.2

 

30. Which individual won a Nobel Prize for his landmark work in sequencing the protein insulin?
  A) Pauling     B) McClintock     C) Gilbert     D) Maxam     E) Sanger
  Ans:  E     Section:  2.2

 

31. Why is the peptide bond planar?
  A) Bulky side chains prevent free rotation around the bond.
  B) It contains partial double-bond character, preventing rotation.
  C) Hydrogen bonding between the NH and C=O groups limits movement.
  D) None of the above.
  E) All of the above.
  Ans:  B     Section:  2.2

 

32. The configuration of most -carbon atoms of amino acids linked in a peptide bond is
  A) cis.     B) circular.     C) parallel.     D) trans.     E) perpendicular.
  Ans:  D     Section:  2.2

 

 

33. What structure(s) did Pauling and Corey predict in 1951?
  A) helix     B) sheet     C) turns     D) a, b, and c     E) a and b
  Ans:  E     Section:  2.4

 

34. 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 above.

  Ans:  C     Section:  2.5

 

35. Where are and turns and loops often found?
  A) in a hydrophobic pocket D) on the surface of proteins
  B) on the interior cleft E) None of the above.
  C) at the protein interface with ligand    
  Ans:  D     Section:  2.3

 

36. What are some of the modifications that proteins acquire?
  A) cleavage and trimming of the protein D) a, b, and c
  B) addition of carbohydrate groups E) b and c
  C) phosphorylation of certain groups    
  Ans:  D     Section:  2.6

 

37. Which of the following amino acid residues would most likely be buried in the interior of a water-soluble, globular protein?
  A) Asp D) Lys
  B) Ser E) Gln
  C) Phe    
  Ans:  C     Section 2.5

 

 

Short-Answer Questions

 

38. How does a proteins amino acid sequence influence the tertiary structure?
  Ans: A protein will spontaneously fold into a three-dimensional structure determined by the amino acid sequence.
  Section:  Introduction

 

39. What is the advantage of having 20 different amino acids available to form proteins?
  Ans: The amino acids provide a rich diversity of functional groups, which can independently contribute to protein structure and function. In addition, many can be modified, increasing the diversity of functional groups.
  Section:  Introduction

 

40. What is the advantage of protein interaction and assembly with other proteins?
  Ans: When proteins interact or assemble, new functions and specificity become available. Protein interactions allow new binding sites at the assembly interface, as well as providing multifunctional activity and specificity, such as found in polymerases and signal transduction.
  Section:  Introduction

 

41. What are the three aromatic amino acids?
  Ans: phenylalanine, tyrosine, and tryptophan
  Section:  2.1

 

42. Which amino acid side chains are capable of ionization?
  Ans: The amino acids are: Asp, Glu, His, Cys, Tyr, Lys, and Arg.
  Section:  2.1

 

43. How does the protein backbone add to structural stability?
  Ans: The protein backbone contains the peptide bond, which has NH molecules and C=O (ketone) groups. Hydrogen-bond formation between the hydrogen on the nitrogen and the oxygen support the protein conformation.
  Section:  2.2

 

44. Why are all the theoretical combinations of phi and psi not possible?
  Ans: Steric hindrances of the side chains make certain combinations and angles impossible.
  Section:  2.2

 

45. Describe some of the features of an helix.
  Ans: The helix is coil stabilized by intrachain hydrogen bonds between the carbonyl oxygen of a residue and the amide hydrogen of the fourth residue away. There are 3.6 amino acids per turn. The hydrogen bonds are between amino acid residues that have two intervening residues.  Thus, these amino acid residues are found on the same side of the coil.  The helix is almost always right-handed, although left-handed helices are, in theory, possible.
  Section:  2.3

 

46. What is the hydrophobic effect as it relates to protein structure?
  Ans: The three-dimensional structure of a water-soluble protein is stabilized by the tendency of hydrophobic groups to assemble in the interior of the molecule.
  Section:  2.1

 

47. Keratin is referred to as a coiled-coil protein. Describe this protein structure.
  Ans: Two or more helices can entwine to form a very stable structure of approximately 100 nm.
  Section:  2.3

 

48. What are prions?
  Ans: Prions are proteins that can assume (after infection or by other causes) a new protein structure, which is self-propagating. The disease has several variants, and at least one is fatal to humans.
  Section:  2.6

 

49. What does the modification involving the attachment of acetyl groups to the amino termini of a protein do?
   Ans: The acetylation of the amino termini of proteins is to make these proteins more resistant to degradation.
  Section:  2.6

 

50. In the ribonuclease experiments performed by Anfinson, what was the significance of the presence of the reducing agent mercaptoethanol?
  Ans: The reducing agent reduced incorrectly paired disulfide bonds, allowing them to reform with the correct pairing until the most stable conformation of the protein had been obtained.
  Section:  2.6

 

51. What is the advantage of having certain regions of partially correct folded regions?
  Ans: If some regions interact preferentially, lending stability to certain conformations as the protein folds, they can impact the overall structure of the protein.
  Section:  2.6

Chapter 16   Glycolysis and Gluconeogenesis

 

 

Matching Questions

Use the following to answer Questions 110:

 

Choose the correct answer from the list below. Not all of the answers will be used.

  1. a) obligate anaerobes
  2. b) AMP
  3. c) Embden Meyerhof pathway
  4. d) NAD+
  5. e) gluconeogenesis
  6. f) UDP-glucose
  7. g) GLUT5
  8. h) facultative anaerobes
  9. i) ATP
  10. j) magnesium
  11. k) galactosemia
  12. l) biotin

 

1. ____________ This is the process by which noncarbohydrate precursor molecules are converted into glucose.

 

  Ans:  e
  Section:  Introduction

 

2. ____________ This is another name for glycolysis.

 

  Ans:  c
  Section:  Introduction

 

3. ____________ These organisms cannot survive in the presence of oxygen.

 

  Ans:  a
  Section:  16.1

 

4. ____________ This substance must be regenerated for glycolysis to proceed.

 

  Ans:  d
  Section:  16.1

 

5. ____________ This intermediate is necessary for the conversion of galactose to glucose.

 

  Ans:  f
  Section:  16.1

 

6. ____________ This molecule is an allosteric inhibitor of phosphofructokinase.

 

  Ans:  i
  Section:  16.2

 

7. ____________ This transporter is responsible for fructose uptake in the intestine.

 

  Ans:  g
  Section:  16.2

 

8. ____________ This condition is a result of a genetic deficiency of a single transferase enzyme.

 

  Ans:  k
  Section:  16.1

 

9. ____________ This essential nutrient is required for the carboxylation of pyruvate in humans.

 

  Ans:  l
  Section:  16.3

 

10. ____________ This is an allosteric inhibitor of gluconeogenesis.

 

  Ans:  b
  Section:  16.4

 

 

Fill-in-the-Blank Questions

 

11. Glycolysis produces a net of ________ moles of ATP per one mole of glucose.
  Ans:  two     Section:  16.1

 

12. Pancreatic ______________ is the digestive enzyme primarily responsible for the hydrolysis of dietary plant starch.
  Ans:  -amylase     Section:  Introduction

 

13. The key enzyme that regulates the pace of glycolysis is ____________________.
  Ans:  phosphofructokinase     Section:  16.1

 

14. The catalytic mechanism of the isomerization of a ketose into an aldose proceeds through an _________________ intermediate.
  Ans:  enediol     Section:16.1

 

15. The formation of ATP is due to direct transfer of a phosphoryl group is called ___________________ .
  Ans:  substrate-level phosphorylation     Section: 16.1

 

16. In alcoholic fermentation, the decarboxylation of pyruvate requires a coenzyme that contains the vitamin ______________.
  Ans:  thiamine, or B1     Section:  16.1

 

17. A potent allosteric activator of liver phosphofructokinase is _____________________, which is produced from fructose-6-phosphate by PFK2.
  Ans:  fructose-2,6-bisphosphate     Section:16.2

 

18. In the absence of oxygen, _____________________ increases the expression of most glycolytic enzymes and the glucose transporters GLUT1 and GLUT3.
  Ans:  HIF-1, or hypoxia-inducible transcription factor,     Section:  16.2

 

19. The ________________ cycle refers to the metabolic reactions by which glucose is converted into lactate in skeletal muscle, and then lactate converted back into glucose in the liver.
  Ans:  Cori     Section:  16.4

 

20. The first step in gluconeogenesis is the ___________________ of pyruvate to form oxaloacetate.
  Ans:  carboxylation     Section:16.3

 

 

Multiple-Choice Questions

 

21. 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) A and B
  E) A, B, and C
  Ans:  D     Section:  Introduction

 

22. What is the purpose of phosphorylating glucose in cytosol?
  A) To trap glucose in the cell
  B) To destabilize glucose and facilitate the next series of metabolic steps
  C) To convert it to a more soluble form
  D) All of the above
  E) A and B
  Ans:  E     Section:  16.1

 

23. What two 3-carbon molecules are generated by the cleavage of fructose-1,6-bisphosphate?
  A) Glyceraldehyde-3-phosphate and 3-phosphoglycerate
  B) Glyceraldehyde-3-phosphate and dihydroxyacetone phosphate
  C) Pyruvate and phosphoenolpyruvate
  D) Enolase and 2-phosphoglycerate
  E) Glyceraldehyde-3-phosphate and pyruvate
  Ans:  B     Section:  16.1

 

24. What is a common mechanistic feature of kinases?
  A) Phosphoryl groups are transferred from a substrate with high phosphoryl-transfer potential to AMP.
  B) Binding of substrate causes a large conformation change that results in cleft closing.
  C) All phosphorylation reactions are specific for monosaccharides.
  D) All of the above.
  E) None of the above.
  Ans:  B     Section:  16.1

 

25. What reaction is catalyzed by aldolase?
  A) Isomerization of DHAP to GAP
  B) Ligation of GAP and DHAP
  C) Reversible cleavage of F-1,6-BP to DHAP and GAP
  D) Cleavage of DHAP to GAP
  E) Irreversible aldol condensation of DHAP and GAP
  Ans:  C     Section:  16.1

 

26. What is the function of glyceraldehyde 3-phosphate dehydrogenase?
  A) Oxidation by NAD+ and formation of acyl-phosphate
  B) Oxidation of the alcohol to an aldehyde
  C) Dehydration and dephosphorylation of GAP
  D) Hydrolysis of GAP
  E) None of the above
  Ans:  A     Section:  16.1

 

27. What is the function of a thioester intermediate such as the one formed from GAP?
  A) It speeds up the actual reaction so that more product can be made.
  B) The thioester shifts the equilibrium of the first stage of the reaction.
  C) The thioester allows the two-step reaction to be coupled so the second reaction, the energetically unfavorable phosphorylation, can proceed.
  D) The thioester intermediate induces a conformational change that alters the enzyme specificity.
  E) The thioester prevents the formation of metabolically unfavorable side products.
  Ans:  C     Section:  16.1

 

28. 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
  Ans:  B     Section:  16.1

 

29. What is the additional metabolite that is required for the conversion of 3-phosphoglycerate to 2-phosphoglycerate?
  A) 1-phosphoglycerate D) 2,3-bisphosphoglycerate
  B) Diacylglycerol E) 1,3-bisphosphoglycerate
  C) NADH    
  Ans:  D     Section:  16.1

 

30. What are the primary metabolic fates of pyruvate?
  A) Eethanol D) All of the above
  B) Lactate E) None of the above
  C) Acetyl CoA    
  Ans:  D     Section:  16.1

 

31. Fructose can enter glycolysis at two distinct points, depending on the tissue. How is fructose metabolized in adipose tissue?
  A) Fructose is cleaved to two molecules of GAP.
  B) Fructose is converted to fructose-1-phosphate.
  C) Fructose is converted to fructose-6-phosphate.
  D) Fructose is cleaved to GAP and DHAP.
  E) Fructose is converted to glucose, which enters the pathway.
  Ans:  C     Section:  16.1

 

32. Lactose intolerance is caused by a deficiency of
  A) lactase.     B) elastase.     C) lactose.     D) sucrase.     E) None of the above.
  Ans:  A     Section:  16.1

 

33. How are the glycolytic enzymes regulated?
  A) Transcriptional control D) All of the above
  B) Teversible phosphorylation E) None of the above
  C) Allosteric control    
  Ans:  D     Section:  16.2

 

34. The primary raw materials for gluconeogenesis are
  A) galactose and sucrose. D) fructose and alanine.
  B) pyruvate and oxaloacetate. E) lactose and lactate.
  C) lactate and alanine.    
  Ans:  C     Section:  16.4

 

35. How many high-energy phosphate bonds are expended in gluconeogenesis?
  A) Three     B) Six     C) Two     D) Four     E) One
  Ans:  B     Section:  16.3

 

 

Short-Answer Questions

 

36. What astounding discovery was made by the Buchners?
  Ans: They were the first to dispute Pasteurs assertion that fermentation required intact cells when they demonstrated that fermentation can occur in yeast extracts.
  Section:  Introduction

 

37. Why do muscles need to generate ATP under aerobic and anaerobic conditions?
  Ans: Muscles initially function aerobically. However, when bursts of energy are required, the oxygen supply does not meet the demand. In order to generate sufficient ATP for energy demands during periods of extreme activity, the muscle depends on activity-dependent anaerobiosis.
  Section:  Introduction

 

38. 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 Km to be higher or lower than hexokinase?
  Ans: Glucokinase must be responsive to elevated blood-glucose concentrations, thus it should have a higher Km.  This lower binding affinity allows this enzyme to become more active at high glucose concentrations, which saturate hexokinase.  Hexokinase serves to phosphorylate glucose (and other hexoses) in the cytosol, and has higher affinity for glucose, or a lower Km value.
  Section:  16.2

 

39. What two isomerization reactions occur in glycolysis? Why are these steps necessary?
  Ans: Glucose-6-phosphate is isomerized to fructose-6-phosphate, converting an aldose to a ketose, which then allows phosphorylation at the number 1 carbon. Later in the pathway, dihydroxyacetone-phosphate is converted to glyceraldehyde-3-phosphate, utilizing both of the molecules formed from fructose-1,6-bisphosphate cleavage.
  Section:  16.1

 

40. At equilibrium, there is far more DHAP than GAP. Yet the conversion of DHAP by triose phosphate isomerase proceeds readily. Why?
  Ans: The GAP formed is immediately removed by subsequent reactions, resulting in conversion of DHAP into GAP by the enzyme.
  Section:  16.1

 

41. How is the conversion of phosphoenolpyruvate to pyruvate accompanied by ATP formation?
  Ans: The enol phosphate possesses very high potential for phosphoryl transfer, which is due to the driving force of the tautamerization of the enol to the more stable ketone.
  Section:  16.1

 

42. Describe the biochemical explanation for galactosemia.
  Ans: Galactose is metabolized by conversion to Gal-1-P by galactokinase.  The enzyme, galactose-1-phosphate uridyl transferase transfers a uridyl group from UDP-Glc to Gal-1-P to produce UDP Gal.  Then UDP-Gal is epimerized to UDP-Glc.  UDP-galactose is a necessary intermediate in the metabolism of galactose.  Individuals deficient in galactose-1-phosphate uridyl transferase activity cannot metabolize galactose, which leads to elevated levels of galactose in the blood and urine.  This genetic disease is referred to as galactosemia.
  Section:  16.1

 

43. Give the reactions by which glycerol (from fats) can be metabolized into pyruvate or synthesized into glucose.
  Ans: After the glycerol is converted into DHAP, it is isomerized into GAP, which can then either proceed down glycolysis to pyruvate or up gluconeogenesis to glucose.
  Section: 16.3

 

44. How is glycolysis maintained under anaerobic conditions?
  Ans: Pyruvate can be reduced to either lactate or ethanol, and this reaction is accompanied by the oxidation of NADH to regenerate NAD+.
  Section:  16.1

 

45. How does citrate influence glycolysis?
  Ans: Phosphofructokinase is inhibited by citrate, which is an intermediate in the citric acid cycle. Thus, if citrate levels are high, the enzyme is inhibited, and fewer glucose molecules are metabolized. In this sense, citrate serves as a cell indicator.  High levels of citrate in the cytoplasm means that biosynthetic precursors are abundant, and so there is no need to degrade additional glucose for this purpose.
  Section: 16.2

 

46. Why is it more sensible for phosphofructokinase to be an important control step, rather than hexokinase?
  Ans: Phosphofructokinase catalyzes the first committed step in the glycolytic pathway. At this point, the molecule is committed to entering the glycolytic path. In contrast, production of G6P is the first step in many different paths. Thus, glycolytic control would not be maintained by tight regulation of hexokinase.
  Section: 16.2

 

47. What two functions are attributed to substrate cycles?
  Ans: The substrate cycles regulate glycolytic path flux by amplifying metabolic signals and they generate body heat produced by the hydrolysis of ATP.
  Section:  16.4

 

48. Which metabolic steps differ from glycolysis in gluconeogenesis?
  Ans: There are three irreversible steps in glycolysis, which require four different steps in gluconeogenesis: pyruvate conversion to phosphoenolpyruvate via an oxaloacetate intermediate, fructose 1,6-bisphosphate hydrolysis, and the hydrolysis of glucose 6-phosphate.
  Section: 16.3

 

49. How are gluconeogenesis and glycolysis regulated reciprocally?
  Ans: The enzymes involved in two substrate cycles are control points. Figure 16.28 in the text shows the glycolytic path activation by F-2,6-BP, AMP, and F-1,6-BP; whereas ATP, alanine, citrate, and protons inhibit glycolysis. Gluconeogenesis is activated by citrate and acetyl CoA and inhibited by F-2,6-BP, AMP, and ADP.
  Section:  16.4

 

50. Describe the two isoforms of lactate dehydrogenase.
  Ans: Two forms exist, called M and H, which predominate in skeletal and heart muscle, respectively. The two forms are products of different genes, but are similar in structure, and can form tetramers in various H:M ratios. The two forms differ in their sensitivity to pyruvate. H4 functions primarily to oxidize lactate to pyruvate, which serves as a fuel for aerobic metabolism. In contrast, M4 produces lactate so that glycolysis can continue under anaerobic conditions.
  Section: 16.4

 

51. During exercise, how is glycolysis regulated by feedforward stimulation.
  Ans: Exercise increases the abundance of fructose-6-phosphate which leads to higher concentrations of fructose-2,6-bisphosphate. Fructose-2,6-bisphosphate increases the affinity of phosphofructokinase for fructose 6-phosphate, leading to an acceleration of glycolysis if glucose is abundant.
  Section: 16.2

 

Chapter 36   Drug Development

 

 

Matching Questions

Use the following to answer Questions 110:

 

Choose the correct answer from the list below. Not all of the answers will be used.

  1. a) ligand
  2. b) beta blocker
  3. c) split pool
  4. d) phase 1
  5. e) Lipinski
  6. f) EC90
  7. g) glucuronic acid
  8. h) phase 3
  9. i) Alexander Fleming
  10. j) Felix Hoffman
  11. k) cGMP
  12. l) cyclooxygenase 2

 

1. ____________ This is the concentration of the drug that gives 90% of the maximum response.

 

  Ans:  f
  Section:  36.1

 

2. ____________ The action of Sildenafil (Viagra) results in an increase of this compound.

 

  Ans:  k
  Section:  36.2

 

 

3. ____________ This set of rules gives a general indication of bioavailability of a drug.

 

  Ans:  e
  Section:  36.1

 

4. ____________ This is a molecule that binds to some target molecule.

 

  Ans:  a
  Section:  36.1

 

5. ____________ This is one of the groups conjugated to drugs to aid excretion.

 

  Ans:  g
  Section:  36.1

 

6. ____________ This enzyme is associated with the inflammatory response.

 

  Ans:  l
  Section:  36.2

 

7. ____________ He is credited with the discovery of penicillin.

 

  Ans:  i
  Section:  36.2

 

8. ____________ This type of synthesis is used in combinatorial chemistry used in drug synthesis.

 

  Ans:  c
  Section:  36.2

 

9. ____________ A popular treatment for hypertension.

 

  Ans:  b
  Section:  36.3

 

10. ____________ Healthy volunteers take the drug for an initial study of safety

 

  Ans:  d
  Section:  36.4

 

 

Fill-in-the-Blank Questions

 

11. Kd corresponds to the concentration of ligand, at which ______________ (fraction?) of the receptors are bound to ligand.
  Ans:  one-half     Section:  36.1

 

12. ________________ is the science that deals with the discovery, chemistry, composition, identification, biological and physiological effects, uses, and manufacture of drugs.
  Ans:  Pharmacology     Section:  Introduction

 

13. A drugs concentration at its target site is affected by its ADME, which is an acronym that stands for _________________________________.
  Ans:  adsorption, distribution, metabolism, and excretion     Section:  36.1

 

14. __________________ is an abundant protein that binds to and transports drugs everywhere the bloodstream flows.
  Ans:  Serum albumin or Plasma albumin     Section:  36.1

 

15. The most notable structural feature of penicillin is a four-membered ring referred to as a ______________ ring.
  Ans:  -lactam     Section:  36.2

 

16. Penicillin inhibits the action of the ____________________ that catalyzes the formation of cross-links in bacterial cell walls.
  Ans:  transpeptidase     Section:  36.2

 

17. Proteins essential for bacterial cell survival are targets of  ___________________ antibiotics.
 

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