Test Bank for Tymoczko Biochemistry A Short Course 3Rd Edition by John L. Tymoczko

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Test Bank for Tymoczko Biochemistry A Short Course 3Rd Edition by John L. Tymoczko

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WITH ANSWERS

 

Tymoczkos Biochemistry A Short Course 3Rd Edition by John L. Tymoczko

Chapter 1            Biochemistry and the Unity of Life

 

 

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) uracil
  2. b) cytoplasm
  3. c) protein
  4. d) thymine
  5. e) carbohydrate
  6. f) sugarphosphate units
  7. g) cell wall
  8. h) transcription
  9. i) glycogen
  10. j) lipid
  11. k) central dogma
  12. l) phagocytosis
  13. m) endoplasmic reticulum
  14. n) translation
  15. o) prokaryotes
  16. p) eukaryotes
  17. q) lysosome

 

1. DNA is made from the building blocks adenine, guanine, cytosine, and ____________.
  Ans: d
  Section: 1.2

 

2. ____________: Unbranched polymer that, when folded into its three-dimensional shape, performs much of the work of the cell.
  Ans: c
  Section: 1.2

 

3. ____________: Scheme that describes the flow of information from one strand of DNA to a new strand of DNA.
  Ans: k
  Section: 1.3

 

4. ____________: Process where large amounts of material are taken into the cell.
  Ans: l
  Section: 1.3

 

5. The transfer of information from DNA to RNA is called ____________.
  Ans: h
  Section: 1.3

 

6. ____________ are cells that are composed of multiple specialized compartments.
  Ans: p
  Section: 1.4

 

7. ____________: Class of biological macromolecules with many functions, such as forming barriers between cell organelles, serving as a metabolic fuel, and cell-to-cell signaling.
  Ans: j
  Section: 1.2

 

8. ____________: Highly organized region of the cell where glycolytic metabolism occurs.
  Ans: b
  Section: 1.4

 

9. ____________: Responsible for protein processing and xenobiotic metabolism.
  Ans: m
  Section: 1.4

 

10.. ____________: Filled with proteases and other digestive enzymes.
  Ans: q
  Section: 1.4

 

Fill-in-the-Blank Questions

 

11. Organisms are known to be highly uniform at the       level.
  Ans: molecular               Section:       Introduction

 

12. After hydrogen and oxygen, the next most common element in living systems is      .
  Ans: carbon                             Section: 1.1

 

13. A chemical that can dissolve in water is said to be      .
  Ans: hydrophilic  Section: 1.2

 

14. A nucleotide consists of one or more       groups, a 5-carbon ribose sugar, and a nitrogen-containing aromatic ring group.
  Ans: phosphoryl            Section: 1.2

 

15. The most common carbohydrate fuel is      .
  Ans: glucose                  Section: 1.2

 

16. Heritable information is packaged into discrete units called      .
  Ans: genes                      Section: 1.3

 

17.  A group of enzymes called      catalyze replication.
  Ans: DNA polymerase            Section: 1.3

 

18. Although all cells in an organism have the same DNA, tissues differ due to selective      .
  Ans: expression             Section: 1.3

 

19. The basic unit of life is considered the      .
  Ans: cell                         Section: 1.4

 

20. Secretory vesicles fuse with the plasma membrane to release material outside of the cell via      .
  Ans: exocytosis             Section: 1.4

 

Multiple-Choice Questions

 

21. The structure of DNA described by Watson and Crick included:
  A) a double helix.
  B) the sugarphosphate backbone aligned in the center of the helix.
  C) the base pairs that are stacked on the inside of the double helix.
  D) A and B.
  E) A and C.
  Ans: E                  Section: 1.2

 

 

22. In higher organisms, which of the following is composed of a polymer with double-stranded phosphodiester-linked monomers?
  A) RNA
  B) DNA
  C) protein
  D) carbohydrate
  E) None of the above.
  Ans: B                  Section 1.2

 

23. What gives proteins such a dominant role in biochemistry?
  A) the variation in protein sizes
  B) the ability to act as a blueprint
  C) their ability to self-replicate
  D) their ability to spontaneously fold into complex three-dimensional structures
  E) All of the above.
  Ans: D                  Section: 1.2

 

24. Proteins are chiefly composed of which of the following?
  A) carbohydrate and amino acids
  B) long unbranched amino acid polymers
  C) peptide bonds formed between lipid moieties
  D) aggregated amino acids
  E) A and B
  Ans: B                  Section 1.3

 

25. How a protein folds is determined by:
  A)  whether the environment is hydrophobic or hydrophilic.

B)   the location in the cell in which the protein is located.

C)   the pH of the cytoplasm.

D)  the order of the amino acids found in the sequence.

E)   All of the above.

  Ans: D                  Section: 1.2

 

 

 

26. The half-life of which of the following is likely to be shortest?
  A) protein

B)  lipid

C)  carbohydrate

D) DNA

E)  RNA

  Ans: E                  Section: 1.2

 

27. The central dogma describes:
  A)  the formation of cells from individual components.

B)   the selective expression of genes.

C)   the flow of information between DNA, RNA, and protein.

D)  the work of polymerases on RNA and DNA.

E)   All of the above.

  Ans: C                  Section: 1.3

 

28. Translation takes place on/in the:
  A)  ribosomes.

B)   smooth endoplasmic reticulum.

C)   nucleus.

D)  DNA polymerases.

E)   DNA parent strand.

  Ans: A                  Section: 1.3

 

29. Which of the following organelles has a double membrane?
  A)  nucleus

B)   endoplasmic reticulum

C)   mitochondria

D)  plasma membrane

E)   A and C

F)    All of the above.

  Ans: E                  Section: 1.4

 

30. The main function of the plasma membrane is to:
  A)  provide the interior of the cell an enclosed environment that no molecules may cross.

B)   provide a selectively permeable barrier with the aid of transport proteins.

C)   give eukaryote and prokaryote cells structural strength.

D)  allow only the free passage of water in and out of the cell.

E)   None of the above.

  Ans: B                  Section: 1.4

 

31. Filaments and microtubules are components of a network called the:
  A)  chloroplast.

B)   cytoplasm.

C)   cytoskeleton.

D)  cell wall.

E)   B and D.

  Ans: C                  Section: 1.4

 

32. Poisons that kill an organism as a result of a loss of high-energy ATP molecules are most likely to target which organelle?
  A)  mitochondria

B)   cytoskeleton

C)   cytoplasm

D)  endoplasmic reticulum

E)   nucleus

  Ans: A                  Section: 1.4

 

33. A secreted protein would be processed through organelles in the following order:
  A)  nucleus; secretory vesicle; Golgi complex.

B)   cytoplasm; Golgi complex; cytosol; secretory vesicle.

C)   endoplasmic reticulum; cytoplasmic reticulum; Golgi complex.

D)  nucleus; cytoplasm; endoplasmic reticulum; Golgi complex; secretory vesicle.

E)   None of the above.

  Ans: E                  Section: 1.4

 

34. Extracellular material is taken into the cell via which process?
  A)  exocytosis

B)   phagocytosis

C)   lysosome-mediated endocytosis

D)  reverse secretory mechanism

E)   phago-cytosolic internalization

  Ans: B                  Section 1.4

 

35. The rigid material that provides structural support to a plant cell is/are called the:
  A)  plant cytoskeleton.

B)   plasma membrane.

C)   cell wall.

D)  chloroplast anchor proteins.

E)   microfilaments and microtubules.

  Ans: C                  Section: 1.4

 

  1. In studying secreted proteins, you find that Substance X inhibits the secretion of a labeled protein. However, you do find a fully synthesized, folded, and glycosylated proteins in the cell. Where is the most likely site in the synthesis and secretion of proteins for Substance X to act?
  2. A) nucleus during translation
  3. B) budding of the secretory granule
  4. C) translation on the ribosome
  5. D) enzyme modification in the Golgi
  6. E) All of the above.

Ans: B                  Section: 1.4

 

  1. Below is the scheme known as the central dogma. Each of the arrows (A, B, C) represents a particular process in gene expression. A, B, and C, respectively, are:

 

  1. A) replication, transcription, translation.
  2. B) reverse transcription, transcription, translation.
  3. C) transcription, translation, replication.
  4. D) replication translation, expression.
  5. E) None of the above.

Ans: A                  Section: 1.3

 

 

  1. Match the loss of a particular organelle with the associated disease.
  2. A) Hypercholesterolemia smooth endoplasmic reticulum
  3. B) Diabetes endosome
  4. C) Tay-Sachs disease lysosome
  5. D) Muscle degeneration mitochondria
  6. E) Stroke Golgi body

Ans: C                  Section: 1.4

 

  1. In a biochemistry lab course, you are asked to design an experiment to identify a strain of bacteria. Your lab partner claims that she thinks the bacterium contains a rough endoplasmic reticulum. To verify her claim, which of the following experiments would you preform?
  2. A) determine whether the bacterium can synthesize ATP in the presence of fuel molecules and O2
  3. B) determine whether the bacterium can synthesize proteins
  4. C) determine whether the bacterium generates CO2 in the presence of fuel molecules
  5. D) determine whether the bacterium has an internal membrane-enclosed compartment
  6. E) All of these experiments will work.

Ans: D                  Section: 1.4

 

Short-Answer Questions

 

40. What are the four key classes of biomolecules?
  Ans: Proteins, DNA/RNA, lipids, carbohydrates. These are the larger, monomer or biopolymer molecules, which perform many functions to maintain cellular life. Each has a different biochemical make-up.
  Section: 1.2

 

41. How do eukaryotic cells differ from prokaryotic cells?
  Ans: The simplest answer is defined by the existence of organelles. Eukaryotic cells contain organelles including a nucleus, while prokaryotic cells do not have such compartments.
  Section: 1.4

 

42. Describe the central dogma and why it is important for cell life.
  Ans: This is the phrase coined by Francis Crick and is the overview of how a cell uses the information from DNA to produce RNA, protein, and more DNA. Much of the fate of a cell (metabolism, survival, growth, movement, and cell differentiation) is based on the control of the central dogma. Which genes are transcribed and translated defines the function of a cell.
  Section: 1.3

 

43. Define an organelle.
  Ans: An organelle is an intracellular compartment, often, but not always, enclosed by a membrane. Examples include the nucleus, mitochondria, and chloroplasts. However, the cytoplasm is defined as that area surrounded by the plasma membrane, excluding the organelles.
  Section: 1.4

 

44. What is the role of the endoplasmic reticulum (ER)?
  Ans: The endoplasmic reticulum is series of membrane tubes or sacs. When studded with ribosomes, the endoplasmic reticulum is considered rough ER and is involved with the processing of nascent protein. Smooth ER is involved in maturing proteins and carbohydrates, and is responsible for xenophobic metabolism of foreign compounds.
  Section: 1.4

 

45. Of the biochemical macromolecules, which class is chiefly responsible for catalysis of cellular processes?
  Ans: Proteins.
  Section: 1.2

 

46. DNA and RNA are composed of what basic biochemical compounds?
  Ans: Both RNA and DNA are nucleotides. Central to nucleotides is a carbohydrate molecule called a ribose or deoxyribose. Bonded to the ribose is one of several aromatic nitrogen-containing organic compounds, which are generically called bases. One or more phosphate groups are also bonded to the ribose or deoxyribose.
  Section: 1.2

 

47. What are the important functions of carbohydrates?
  Ans: Structural, energy storage, modify proteins, cellcell recognition..
  Section: 1.2

 

48. What is significant about the DNA process of replication?
  Ans: It provides a mechanism for copying the DNA from one generation to the next.
  Section: 1.4

 

 

49. Which property of lipids drives the formation of membranes?
  Ans: The dual chemical nature of lipids allows them to self-organize into membranes.
  Section: 1.2

 

  1. What data might Monod cite to justify the phrase Anything found to be true of E. coli must also be true of elephants?

Ans: He would most likely describe similarities between eukaryotic and prokaryotic cells. The first is a barrier, a membrane, that separates the cell form its environment such that independent of cell type, the interior of the cell is chemically different that the external environment. The membrane is more than a barrier; it is selectively permeable and directs the flow of molecules into and out of the cell. The second is the structure of the molecule that carries information regarding cell activities as the cell undergoes duplication each generation. Nucleic acids are the information storage molecule for living systems.

Chapter 3 Amino Acids

 

 

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. Answers may be used more than once.

  1. a) l amino acids
  2. b) water
  3. c) protons
  4. d) zwitterions
  5. e) arginine
  6. f) serine
  7. g) tyrosine
  8. h) cysteine
  9. i) glutamate
  10. j) histidine
  11. k) proline
  12. l) asparagine
  13. m) d amino acids

 

1. ____________: Chiral type of amino acids found in proteins.
  Ans: a
  Section: 3.1

 

2. ____________: Another name for dipolar molecules.
  Ans: d
  Section: 3.1

 

3. ____________: Disulfide bonds are formed by pairs of this amino acid.
  Ans: h
  Section: 3.2

 

4. ____________: The amino acid with a side-chain pKa just below neutral pH.
  Ans: j
  Section: 3.2

 

5. ____________: The amino acid with a side group that has a terminal carboxamide.
  Ans: l
  Section: 3.2

 

6. ____________: The amino acid with an imidazole side chain.
  Ans: j
  Section: 3.2

 

7. ____________: An amino acid that must be supplied by the diet.
  Ans: j
  Section: 3.3

 

8. ____________: The amino acid with a negatively charged side chain at neutral pH.
  Ans: i
  Section: 3.2

 

9. ____________: The amino acid with a sulfhydryl side chain.
  Ans: h
  Section: 3.2

 

10. ____________: The amino acid with the abbreviation Ser.
  Ans: f
  Section: 3.2

 

Fill-in-the-Blank Questions

 

11. The amino acid that contains a weakly acidic phenolic group is      .
  Ans: tyrosine               Section 3.2

 

12.       are amino acids with neutral R groups containing an electronegative atom.
  Ans: Polar amino acids            Section 3.2

 

13. The amino acid with the smallest-size side chain allowing greatest flexibility in a protein is      .
  Ans: glycine                 Section 3.2

 

14. The charge of glycine when the pH is < 2.0 is      .
  Ans: +1                        Section 3.1

 

15. Between the amino and the carboxyl functional group, the       has the lowest affinity for a proton.
  Ans: carboxyl              Section: 3.1

 

16. The amino acid with an indol ring is      .
  Ans: tryptophan                       Section: 3.2

 

17.        is an amino acid with a hydrophobic side chain containing a thioether.
  Ans: Methionine                      Section: 3.2

 

18. The       group is the functional group that makes an amino acid more reactive than nonpolar amino acids such as valine, alanine, and phenylalanine.
  Ans: hydroxyl              Section: 3.2

 

19.  
  Ans: nonessential         Section: 3.3

 

20.       is often seen in a child with a protein-deficient diet.
  Ans: Edema                 Section: 3.3

 

Multiple-Choice Questions

 

21. What charged group(s) is/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: 3.2

 

22. At a pH of 12, what charged group(s) is/are present in glycine?
  A) NH3+
  B) COO
  C) NH2+
  D) A and B
  E) A, B, and C
  Ans:  B            Section:  3.2

 

23. In what pH range is zwitterionic alanine the predominate structure?
  A) 02
  B) 914
  C) 810
  D) 24
  E) 29
  Ans:  E     Section 3.2

 

24. Which amino acids contain reactive aliphatic hydroxyl groups?
  A) serine and methionine
  B) serine and threonine
  C) methionine and threonine
  D) cysteine and methionine
  E) cysteine and threonine
  Ans: B             Section: 3.2

 

25. Name three amino acids that are positively charged at a neutral pH.
  A) lysine and arginine
  B) histidine and arginine
  C) cysteine and arginine
  D) lysine and proline
  E) glutamine and histidine
  Ans: A             Section: 3.2

 

26. What would interactions between side chains of aspartate and arginine at neutral pH be?
  A) hydrophobic
  B) ionic
  C) hydrogen bonding
  D) steric
  E) covalent
  Ans: B             Section: 3.2

 

27. Which amino acid has a side chain with a hydroxyl group?
  A) serine
  B) alanine
  C) tryptophan
  D) histidine
  E) glutamine
  Ans: A             Section: 3.2

 

28. Which amino acid has a carboxyl group in its side chain?
  A) glutamine
  B) galanine
  C) cysteine
  D) glutamate
  E) None of the above.
  Ans: D             Section: 3.2

 

29. What would the overall charge of a peptide of the following peptide sequence at pH 1 be (Asp-Gly-Arg-His)?
  A) 1
  B) 0
  C) 1
  D) 2
  E) 3
  Ans: E              Section: 3.2

 

30. Which of the following amino acids would most likely be soluble in a nonpolar solvent such as benzene?
  A) valine
  B) histidine
  C) glutamine
  D) glycine
  E) All of the above.
  Ans: A             Section: 3.2

 

31. Below is a list of five tripeptides identified by their single letter codes. They are listed as A, B, C, D, and E. Which tripeptide contains an amino acid capable of forming covalent disulfide bonds?
  A) FNC
  B) RGK
  C) VIL
  D) MDE
  E) SYT
  Ans: A             Section: 3.2

 

32. Below is a list of five tripeptides identified by their single letter codes. They are listed as A, B, C, D, and E. Which tripeptide is negatively charged at physiological pH?
  A) FNC
  B) RGK
  C) VIL
  D) MDE
  E) SYT
  Ans: D             Section: 3.2

 

33. Below is a list of five tripeptides identified by their single letter codes. They are listed as A, B, C, D, and E. Which tripeptide has the most polar side chains?
  A) FNC
  B) RGK
  C) VIL
  D) MDE
  E) SYT
  Ans: E              Section: 3.2

 

34. Where are Trp and Phe found in a globular protein and why?
  A)  exterior due to the hydrophilic effect
  B) interior due to the hydrophobic effect
  C) exterior forming polar H-bonds with water
  D) interior forming ionic bonds with other amino acids
  E) exterior forming ionic-polar bonds with water
  Ans: B             Section: 3.2

 

35. Amino acids contain all of the following functional groups except:
  A) indole.
  B) thioester.
  C) phenyl.
  D) sulfhydryl.
  E) amine.
  Ans: B             Section: 3.2

 

Short-Answer Questions

 

36. What is the advantage of having multiple functional groups in proteins?
  Ans: The rich diversity of functional groups in proteins can contribute independently to protein structure and accounts for the diversity in function as well.
  Section: Introduction

 

37. What is the advantage of protein interaction and assembly with other proteins?
  Ans: When proteins interact or assemble, new functions and specificity become available. These protein interactions provide multifunctional activity and specificity.
  Section: Introduction

 

38. Draw the general structure of an amino acid at pH 7.0 with the side group shown as an R.
  Ans: The figure should look like either one of the structures shown in the left margin on p. 38.
  Section: 3.1

 

39. Why is the central carbon on an amino acid so important?
  Ans: This is the chiral center of the molecule and is linked to each important functional group of an amino acid.
  Section: 3.1
40. Draw the structure of alanine, aspartic acid, and histidine when the pH is 1.0, 7.0, and 12.0.
  Ans: Use the figures in your book and the pKa for each functional group to determine the ionization state for each amino acid.
  Section: 3.2

 

41. What is the net charge of each the following amino acid: alanine, aspartic acid, and histidine when the pH is 1.0, 7.0, and 12.0?
  Ans: For alanine, the charges are: 1, 0, and 1. For aspartic acid, the charges are: 1, 1, and 2. For histidine, the charges are: 2, 0, and 1.
  Section: 3.2

 

42. A gene is mutated so the amino acids glycine and glutamate are now alanine and leucine, respectively. What are the potential results of each of these mutations? Assume that the mutations are not near each other in the primary sequence and have no impact on the other.
  Ans: The glycine-to-alanine mutations are similar and will have little or no effect. Glutamate and leucine have very different chemistries and will impact the function and structure of the protein, as one is charged and water soluble, and the other is hydrophobic and nonpolar.
  Section: 3.2

 

43. What are the four ways amino acids can be classified?
  Ans: hydrophobic, polar, positively charged, and negatively charged
  Section: 3.2

 

44. What are the three aromatic amino acids?
  Ans: phenylalanine, tyrosine, and tryptophan
  Section: 3.2

 

45. Which amino acid side chains are capable of ionization?
  Ans: The amino acids are aspartate, glutamate, histidine, cysteine, tyrosine, lysine, and arginine.
  Section: 3.2

 

46. Which are the branched amino acids, and what impact do they have on protein shape?
  Ans: These are the aliphatic, hydrophobic amino acids, valine, leucine, and isoleucine. They are hydrophobic, which drives the hydrophobic interactions in the interior of a protein. These are also bulky amino acids that will lend to steric strain if forced close to each other in a peptide.
  Section: 3.2

 

47. Draw a titration curve for glycine.
  Ans: Use the information from Section 2.5 and the graph from Figure 3.2.
  Section: 3.2

 

48. What do serine, threonine, and tyrosine have in common?
  Ans: Each has a hydroxyl (OH) group, which makes the first two amino acids more water soluble and increases the reactivity of all three amino acids.
  Section: 3.2

 

49. Which amino acid is responsible for stabilizing the structure of a protein by forming pairs of sulfhydryl groups?
  Ans: cysteine
  Section: 3.2

 

50. What functions make histadine an important amino acid?
  Ans: The pKa of the imidazole ring is near physiological pH. This means that the side group may be charged and protonated or neutral and deprotonated. This results in an amino acid that can either lend or accept a proton or charge in the active site of an enzyme.
  Section: 3.2

 

51. Which amino acids have a side chain that includes a modified carboxyl group, carboxaminde?
  Ans: asparagine and glutamine
  Section: 3.2

 

52. Which ionizable group has the lowest affinity for protons: the terminal a-carboxyl group, the aspartic acid side group, or the terminal a-amino group?
  Ans: the terminal a-carboxyl group
  Section: 3.2

 

53. Malnourished children with Kwashiorkor display a distended stomach, giving the illusion of being full. Why does this happen?
  Ans: This is a nutritional state where there is an extremely low or poor protein intake in the diet. The osmolar shift of the blood, which is poor in protein content, causes water to flow into the tissues.
  Section: 3.3

 

54. What is the difference between nonessential and essential amino acids?
  Ans: The former are amino acids that humans can generate de novo, or from scratch. The latter cannot be made and must be ingested for the mature formation of proteins.
  Section: 3.3

 

55. List the essential amino acids.
  Ans: histadine, isoleucine, leucine, lysine, methionine, phenylalanine, threonine, tryptophan, and valine
  Section: 3.3

Chapter 11   Lipids

 

 

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) ether-linked lipid
  2. b) triacylglycerol
  3. c) sterol
  4. d) amphipathic
  5. e) 16 or 18
  6. f) organic solvent
  7. g) cholesterol
  8. h) cysteine
  9. i) phospholipid
  10. j) prokaryotes
  11. k) glycolipid
  12. l) 20 or 24
  13. m) sphingosine
  14. n) serine

 

1. ____________ The storage form of fatty acids.

 

  Ans:  b
  Section:  Introduction

 

2. ____________ This is the number of carbons in most common fatty acids.

 

  Ans:  e
  Section:  11.1

 

3. ____________ In addition to phospholipids and glycolipids, this is a major type of membrane lipid.

 

  Ans:  g
  Section:  11.3

 

4. ____________ This is a term applied to molecules that have both hydrophilic and hydrophobic moieties.

 

  Ans:  d
  Section:  11.3

 

5. ____________ A lipid is defined as a compound soluble in ________________.

 

  Ans:  f
  Section:  Introduction

 

6. ____________ Lipids that are bound to carbohydrates.
  Ans:  k
  Section:  Introduction

 

7. ____________Type of lipid with two acyl chains, a glycerol backbone, and a polar head group.
  Ans:  i
  Section:  11.3

 

8. ____________ Flat polycylic molecule absent in prokaryotic membranes.

 

  Ans:  g
  Section:  11.3

 

9. ____________ These lipids are less resistant to hydrolysis, potentially due to the way the acyl chain is linked to the glycerol backbone.

 

  Ans:  a
  Section:  11.3

 

10. ____________ A complex amino alcohol backbone for membrane lipids.

 

  Ans:  m
  Section:  11.3

 

 

Fill-in-the-Blank Questions

 

11.      is a membrane lipid composed of sphingosine, fatty acid, and a simple sugar.
  Ans:  Cerebroside     Section:  11.3

 

12. The common name of hexadecanoic acid is      .
  Ans:  palmitic acid     Section:  11.1

 

13. In phosphoglycerides, the fatty acids are linked to the glycerol backbone by the       linkages.
  Ans:  ester     Section:  11.3

 

14. The configuration of most fatty acids in biological systems is      .
  Ans:  cis     Section:  11.1

 

15. Fatty acids are ionized at physiological pH and so are referred to in their      form.
  Ans:  carboxylate     Section:  11.1

 

16.      The short-hand notation indicating that there are two cis double bonds between carbons 9 and 10 and again between 12 and 13.
  Ans:  cis, cis-9,12   Section:  11.1

 

17. The presence of double bonds in fatty acids limits tight packaging and the number of

      interactions.

  Ans:  van der Waals     Section:  11.1

 

18.       is the type of glycolipid that contains a branched chain of as many as seven sugar residues.
  Ans: Ganglioside   Section:  11.3

 

19. The reduction in tight packing due to cis double bonds       the melting temperature of a fatty acid.
  Ans: lowers   Section:  11.1

 

20. One important       is EPA (eicosapentoenoate) and is found in fatty fish and shellfish.
  Ans:  -3 fatty acid   Section:   11.1

 

 

Multiple-Choice Questions

 

21. Membrane lipids are primarily comprised of:
  A) phospholipids.     B) glycolipids.     C) cholesterol.     D) A and B.     E) A, B, and C.
  Ans:  E     Section:  11.3

 

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22.  Which of the following is NOT a main function of lipids?
  A) cell signaling