Biochemistry, 6th Edition Reginald Garrett - Test Bank
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Biochemistry, 6th Edition Reginald Garrett - Test Bank

Biochemistry, 6th Edition Reginald Garrett - Test Bank   Instant Download - Complete Test Bank With Answers     Sample Questions Are Posted Below   1. A gene can be defined as:   a. the unique function that some cells have but other cells do not have.   b. a specific segment of nucleotide bases in …

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Biochemistry, 6th Edition Reginald Garrett – Test Bank

 

Instant Download – Complete Test Bank With Answers

 

 

Sample Questions Are Posted Below

 

1. A gene can be defined as:

  a. the unique function that some cells have but other cells do not have.
  b. a specific segment of nucleotide bases in DNA that encode for the synthesis of a particular protein.
  c. a single strand of DNA that is designated as the sense strand.
  d. a functional segment of a unique protein.
  e. the segment of DNA that is changed in a mutation.

 

ANSWER:   b

 

2. Proteins with two different polypeptide chains are:

  a. monomeric proteins.
  b. trimeric proteins.
  c. homodimeric proteins.
  d. heterodimeric proteins.
  e. none of the above.

 

ANSWER:   d

 

3. Hemoglobin is an α2, β2 ____ whereas, glutamine synthetase from E. coli is an α12 ____.

  a. -homodimer, -homomultimer
  b. -heteromultimer, -homomultimer
  c. -homomultimer, -heterodimer
  d. -heterodimer, -monomeric protein
  e. -heterodimer, -homomultimer

 

ANSWER:   b

 

4. Fibrous proteins, such as collagen, have which one of the following properties?

  a. Highly soluble in water.
  b. Their hydrophilic residues are directed into the interior of the protein.
  c. Exhibit enzymatic activity.
  d. Serve structural roles in the cell.
  e. Monomeric.

 

ANSWER:   d

 

5. Which of the following IS NOT a characteristic of globular proteins?

  a. Insoluble in water.
  b. Roughly spherical.
  c. Folded so that the hydrophobic amino acids are in the interior of the molecule.
  d. Hydrophobic side chains are exposed to the water.
  e. None, all are true.

 

ANSWER:   a

 

6. Molecules of a given protein have all EXCEPT:

  a. a fixed amino acid composition.
  b. a defined amino acid sequence.
  c. a sequence read from C-terminal end to N-terminal end.
  d. an invariant molecular weight.
  e. a nucleotide sequence from which they are encoded.

 

ANSWER:   c

 

7. Membrane proteins differ from globular proteins in that:

  a. membrane associated amino acids usually have polar side chains.
  b. membrane proteins are much more soluble in detergents than water.
  c. membrane proteins usually have more hydrophobic amino acids.
  d. globular proteins are water insoluble.
  e. All are true.

 

ANSWER:   b

 

8. A common reaction of two cysteine residues in proteins results in the formation of ____.

  a. thioester bonds
  b. disulfide bonds
  c. dithiol bonds
  d. thioether bonds
  e. none of the above

 

ANSWER:   b

 

9. The amino acid sequence is defined as ____ structure.

  a. primary
  b. secondary
  c. tertiary
  d. quaternary
  e. all are true

 

ANSWER:   a

 

10. α-Helix and β-strand are components of ____ structure

  a. primary
  b. secondary
  c. tertiary
  d. quaternary
  e. all are true

 

ANSWER:   b

 

11. All of the information necessary for a protein to achieve its intricate architecture is contained within its ____ structure.

  a. primary
  b. secondary
  c. tertiary
  d. quaternary
  e. all are true

 

ANSWER:   a

 

12. The formation of a disulfide bond would be an example of what level of protein structure?

  a. primary
  b. secondary
  c. tertiary
  d. quaternary
  e. both c and d are correct

 

ANSWER:   e

 

13. Which of the following IS NOT a characteristic of a protein’s overall conformation?

  a. The overall three-dimensional architecture of the protein.
  b. Achieved by breaking and reforming covalent bonds.
  c. Achieved by rotations about each single bond along the peptide backbone.
  d. The result of amino acid side-chain interactions.
  e. None, all are true.

 

ANSWER:   b

 

14. Which of the following levels of protein structure is correctly defined?

  a. primary: interaction between subunits of a protein
  b. secondary: hydrogen bond arrangement of polar R-groups
  c. tertiary: three dimensional arrangement of all atoms in a single peptide
  d. quaternary: order of amino acid residues in the peptide chain
  e. none of the above are correct

 

ANSWER:   c

 

15. Which of the following is not a commonly used technique for protein isolation and purification?

  a. gas-liquid chromatography.
  b. ion exchange chromatography.
  c. electrophoresis.
  d. solubility (“salting in” and “salting out”).
  e. affinity chromatography.

 

ANSWER:   a

 

16. Even though acid hydrolysis of proteins is favored over basic hydrolysis, with acid hydrolysis ____ is destroyed and must be estimated by other means.

  a. Lys
  b. Leu
  c. Asp
  d. Cys
  e. Trp

 

ANSWER:   e

 

17. Amino acid analysis of a protein gives:

  a. the sequence of the protein.
  b. the number of residues of each amino acid in the protein.
  c. the molecular weight of the protein.
  d. the percentage or ratio of the various amino acids in the protein.
  e. an identification of the N-terminal and C-terminal amino acids.

 

ANSWER:   d

 

18. The amino acid sequence is NOT:

  a. a distinctive characteristic of a polypeptide.
  b. encoded by the nucleotide sequence of DNA.
  c. a form of genetic information.
  d. read from N-terminal end to C-terminal end.
  e. constant for proteins with the same function from different organisms.

 

ANSWER:   e

 

19. Edman degradation will:

  a. determine the C-terminal amino acid by using a carboxypeptidase.
  b. cleave the protein into a multitude of smaller peptides.
  c. compare overlapping sets of peptide fragments.
  d. determine the N-terminal amino acid.
  e. generate two different, but overlapping sets of peptide fragments.

 

ANSWER:   d

 

20. After treating a protein with trypsin, which of the following techniques could be used to determine its identity by peptide mass fingerprinting?

  a. NMR
  b. MALDI-TOF mass spectrometer
  c. HPLC
  d. gel electrophoresis
  e. none of the above

 

ANSWER:   b

 

21. Reaction of the peptide, ala-met-lys-ser, with phenylisothiocyanate (PITC) at pH 8.0 followed by mild acidification (first cycle of Edman method) would release:

  a. the labeled peptide ala-met-lys-ser-PTH.
  b. PTH-ala, PTH-ser, PTH-lys and PTH-met.
  c. PTH-ser and the peptide ala-met-lys.
  d. PTH-ala and the peptide met-lys-ser.
  e. All of the above.

 

ANSWER:   d

 

22. What is the product formed from the acid hydrolysis of a simple amide?

  a. acid & base
  b. aldehyde & alcohol
  c. acid & amine
  d. ester & alcohol
  e. amine & aldehyde

 

ANSWER:   c

 

23. Which of the following would not be a useful procedure for dissociating the subunits of a multimeric protein in order to sequence the individual subunits?

  a. Exposure to pH extremes (ie, pH 1 or pH 13).
  b. High salt concentrations.
  c. 6 N HCl at 110°C for 24 hours.
  d. 8 M urea.
  e. 6 M guanidinium chloride.

 

ANSWER:   c

 

24. Insulin is a polypeptide hormone that contains two short polypeptide chains linked by two interstrand disulfide bonds. The most logical order of events to perform in order to sequence this protein would be:

A. The peptides are reduced with mercaptoethanol.
B. The peptides are sequenced using Edman chemistry.
C. The peptides are separated by chromatography techniques.
D. The peptides are alkylated with iodoacetamide.

 

  a. A, D, C, B
  b. C, A, D, B
  c. C, B, A, D
  d. A, B, C, D
  e. A, C, D, B

 

ANSWER:   a

 

25. The C-terminal residue of a polypeptide can be determined by first cleaving the polypeptide with:

  a. chymotrypsin.
  b. carboxypeptidase.
  c. trypsin.
  d. CNBr.
  e. none of the above.

 

ANSWER:   b

 

26. ____ is specific in hydrolyzing only peptide bonds in which the carboxyl function is contributed by an arginine or a lysine residue.

  a. Chymotrypsin
  b. Carboxypeptidase
  c. Trypsin
  d. CNBr
  e. None of the above.

 

ANSWER:   c

 

27. The advantage of treating separate samples of a protein with two or more enzymes when sequencing a protein is that the products are:

  a. more homogeneous.
  b. sequenceable without further chromatography.
  c. fragments with the same N- and C-terminal amino acids.
  d. fragments with sequence overlaps.
  e. all are true.

 

ANSWER:   d

 

28. What is the overall net charge on the peptide lys-lys-ser-glu at pH 7.0?

  a. +2
  b. +1
  c. 0
  d. −1
  e. −2

 

ANSWER:   b

 

29. All of the statements about the peptide val-asp-trp-asn-ser are correct EXCEPT:

  a. This peptide would show a strong absorption band at 280 nm.
  b. Reaction with chymotrypsin would yield two peptides.
  c. To synthesize this peptide using the solid phase method of Merrifield, the amino acid directly attached to the resin would be valine.
  d. After the second round of Edman degradation using the reagent PITC, the PTH-amino acid residue released would be PTH-asp.
  e. The peptide would be converted to a dipeptide and a tripeptide by chymotrypsin.

 

ANSWER:   c

 

30. Which of the following would be a possible amino acid sequence for an oligopeptide given the experimental data below?

1. The amino acid composition is found to be [ala, lys, phe, met, cys, plus some decomposition products].
2. The peptide has a molecular weight around 700 Da and absorbs at 280 nm.
3. Treatment with carboxypeptidase results in tryptophan and a peptide.
4. CNBr treatment yields a tetrapeptide and a dipeptide.
5. Trypsin digestion produces an amino acid and a pentapeptide with met on the amino end.
6. Chymotrypsin digestion yields a dipeptide and a tetrapeptide.

 

  a. trp-lys-met-cys-met-ala
  b. lys-met-cys-phe-ala-trp
  c. trp-ala-phe-cys-met-lys
  d. lys-ala-cys-phe-met-trp
  e. lys-met-cys-ala-phe-trp

 

ANSWER:   b

 

31. The preponderance of protein sequence information is now derived from:

  a. chemical sequencing (Edman method).
  b. mass spectrometry.
  c. mass spectrometry-mass spectrometry.
  d. translating the nucleotide sequence of genes into codons, and thus amino acid sequence.
  e. none of the above.

 

ANSWER:   d

 

32. Homologous proteins such as hemoglobin from different organisms do NOT:

  a. have nearly identical lengths.
  b. share little sequence homology with other proteins with similar function (e.g., myoglobin).
  c. share a significant degree of sequence similarity.
  d. perform the same function in different organisms.
  e. have sequence identity in direct correlation to the relatedness of the species from which they were derived.

 

ANSWER:   b

 

33. Although they have very different functions, hen egg white lysozyme and ____ share similar sequence homology and similar tertiary structure.

  a. trypsin
  b. α-lactalbumin
  c. thrombin
  d. hemoglobin
  e. chymotrypsin

 

ANSWER:   b

 

34. The diversity in hemoglobin mutants indicates that:

  a. any amino acid change is relatively important.
  b. any amino acid change is lethal to the organism.
  c. specific amino acid changes drastically alter one or more functions of a protein.
  d. any amino acid change will have the same effect on the protein function.
  e. All are true.

 

ANSWER:   c

 

35. Proteins destined for an extracellular location are characteristically:

  a. phosphoproteins.
  b. glycoproteins.
  c. lipoproteins.
  d. nucleoproteins.
  e. flavoproteins.

 

ANSWER:   b

 

36. Proteins that do NOT perform any obvious chemical transformation, but control the ability of other proteins to carry out their physiological functions are:

  a. enzymes.
  b. regulatory proteins.
  c. transport proteins.
  d. storage proteins.
  e. structural proteins.

 

ANSWER:   b

 

37. Hemoglobin is an example of a(n):

  a. enzyme.
  b. regulatory protein.
  c. transport protein.
  d. storage protein.
  e. structural protein.

 

ANSWER:   c

 

38. Collagen is an example of a(n):

  a. enzyme.
  b. regulatory protein.
  c. transport protein.
  d. storage protein.
  e. structural protein.

 

ANSWER:   e

 

39. Which of the following reagents is correctly defined?

  a. iodoacetic acid:  reduces disulfide bonds
  b. guanadinium hydrochloride:  disrupts ionic interactions and hydrogen bonds
  c. phenylisothiocyanate:  reacts with free carboxyl groups
  d. cyanogen bromide:  reacts with internal cysteine residues
  e. performic acid:  reacts with free cysteine residues

 

ANSWER:   b

 

40. Which of the following protease enzymes is correctly identified with its specificity?

  a. trypsin:  cleaves on C-side of acidic amino acids
  b. chymotrypsin:  cleaves on C-side of aliphatic amino acids
  c. staphylococcal protease:  cleaves on C-side of acidic amino acids
  d. clostripain:  cleaves on C-side of lysine
  e. none of the above are correct

 

ANSWER:   c

 

41. Which of the following amino acids occurs most frequently in proteins?

  a. methionine
  b. alanine
  c. tryptophan
  d. tyrosine
  e. histidine

 

ANSWER:   b

 

42. Which of the following mutations would probably be least likely to impact the function of the protein?

  a. Lys to Ser
  b. Ala to Asp
  c. His to Pro
  d. Val to Ile
  e. Phe to Tyr

 

ANSWER:   d

 

43. Discuss the quaternary structure of proteins with an example.​

ANSWER:   Many proteins consist of two or more interacting polypeptide chains of characteristic tertiary structure, each of which is commonly referred to as a subunit of the protein. Subunit organization constitutes another level in the hierarchy of protein structure, defined as the protein’s quaternary (4°) structure. Questions of quaternary structure address the various kinds of subunits within a protein molecule, the number of each, and the ways in which they interact with one another. The α and β polypeptide chains of hemoglobin interact to form a quaternary structure.​
TOPICS:   5.1 What Architectural Arrangements Characterize Protein Structure?

 

44. ​Explain the role of trypsin in identifying the primary structure of a protein.

ANSWER:   Trypsin is a digestive enzyme that is used to produce polypeptide fragments useful for sequence analysis. Trypsin is the most commonly used reagent for specific proteolysis. Trypsin will only hydrolyze peptide bonds in which the carbonyl function is contributed by an arginine or a lysine residue. That is, trypsin cleaves on the C-side of Arginine (Arg) or Lysine (Lys), generating a set of peptide fragments having Arg or Lys at their C-termini. The number of smaller peptides resulting from trypsin action is equal to the total number of Arg and Lys residues in the protein plus one—the protein’s C-terminal peptide fragment.​
TOPICS:   5.4 How Is the Primary Structure of a Protein Determined?

 

45. Discuss the computer programs that can align amino acid sequences.​

ANSWER:   Protein sequence databases provide enormous resources for sequence comparisons. If two proteins share homology, it can be revealed through alignment of their sequences using powerful computer programs. In such studies, a given amino acid sequence is used to query the databases for proteins with similar sequences. BLAST (Basic Local Alignment Search Tool) is a commonly used program for rapid searching of sequence databases. The BLAST program detects local as well as global alignments where sequences are in close agreement. Even regions of similarity shared between otherwise unrelated proteins can be detected. Discovery of sequence similarities between proteins can help to guess the function of uncharacterized proteins and also to assign related proteins to protein families.​
TOPICS:   5.5 What Is the Nature of Amino Acid Sequences?

 

46. Discuss the biological functions of proteins.​

ANSWER:   Proteins fill essentially every biological role, with the exception of information storage. Binding proteins typically interact noncovalently with their specific ligands. Transport proteins—a class of binding proteins—include membrane proteins that transport substances across membranes, as well as soluble proteins that deliver specific nutrients or waste products throughout the body. Scaffold proteins are also binding proteins that use protein–protein interactions to recruit other proteins into multimeric assemblies that mediate and coordinate the flow of information in cells. Catalytic proteins (enzymes) mediate many metabolic reactions. Regulatory proteins that bind to specific nucleotide sequences within DNA control gene expression. Hormones—a kind of regulatory proteins—convey information about the environment to cells when they bind to specific receptors.​
TOPICS:   5.8 What Are the Many Biological Functions of Proteins?

 

47. Explain the significance of the proteome.​

ANSWER:   An accurate reflection of what a cell is doing at any moment in time is found in the proteome because proteins are the agents of cellular function. The full genetic potential of a cell (what it is capable of doing) is contained within its genome, but not all genes are expressed at any moment in time. The proteome is much more complex than the genome. While there are only 20,000 or so protein-coding genes in the human genome, estimates suggest that there are hundreds of thousands of different proteins, perhaps even a million or more. This discrepancy exists because one gene may give rise to a large number of protein products through a range of processes, such as post-translational modification or alternative RNA splicing or RNA editing.​
TOPICS:   5.9 What Is the Proteome and What Does It Tell Us?

 

 

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