Biochemistry 9th Edition Campbell - Test Bank Instant Download - Complete Test Bank With Answers Sample Questions Are Posted Below 1. What tends to happen to the percent recovery during a protein's purification? a. The number usually steadily increases during the purification. b. The number usually steadily decreases during the …
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Biochemistry 9th Edition Campbell – Test Bank
Instant Download – Complete Test Bank With Answers
Sample Questions Are Posted Below
1. What tends to happen to the percent recovery during a protein’s purification?
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2. Differential centrifugation at low speeds (several thousand RPM) is a useful step when
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3. The typical order for the major steps of enzyme isolation would be (from first to last):
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4. The purity of an enzyme at various stages of purification is best measured by
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5. Salting out with ammonium sulfate is based upon proteins interacting with other proteins via
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6. Using differential centrifugation it is possible to separate
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7. The following methods are useful for cell homogenization:
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8. Which of the following happens as a protein is purified?
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9. Ammonium sulfate is useful in protein purification because
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10. The typical order of differential centrifugation for organelles is (from slowest speed/lowest g to fastest speed/highest g):
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11. Which of the following are principles on which to base column chromatography?
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12. Which separates on the basis of molecular weight?
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13. Which separates based on the ionic charge on a protein?
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14. Which type of column is most affected by the shape of the protein, for example, comparing spherical and cigar-shaped proteins?
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15. Which would be best to separate a protein that binds strongly to its substrate?
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16. Elution of proteins by means of a pH gradient would work best with this type of column:
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17. Which would be best to separate positively charged proteins?
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18. Which would be best to separate proteins of similar size?
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19. In affinity chromatography, a protein
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20. In gel filtration chromatography
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21. The order of elution of AAs H, E, & K from a cation exchange column by a pH 6 buffer is
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22. In any form of chromatography, how will a compound which interacts more strongly with the stationary phase elute compared to one that interacts less strongly?
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23. A chromatography technique where a solution of nonpolar compounds is put through a column that has a nonpolar liquid immobilized on an inert matrix is which type of chromatography?
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24. In a sample consisting of lysine, leucine, and glutamic acid, which will be eluted last from an anion exchange resin at pH 7?
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25. In chromatography the experimental setup always requires
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26. A separation of a mixture of cations of different charge requires
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27. Which of the following is not an example of column chromatography?
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28. In affinity chromatography
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29. The degree of separation in molecular sieve chromatography depends on
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30. In all forms of chromatography one way of identifying eluted substances is by
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31. Which substance would you expect to be eluted first from a molecular sieve column with a suitable degree of crosslinking?
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32. In the SDS-PAGE (sodium dodecylsulfate – polyacrylamide gel electrophoresis) method, separation takes place on the basis of
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33. How many bands would be produced when hemoglobin is subjected to SDS-PAGE?
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34. The following are all principles on which to base electrophoresis except:
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35. Two-dimensional electrophoresis usually exploits these 2 different properties of proteins:
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| Exhibit 5A The following diagram shows the anode, cathode, and pH gradient of an isoelectric focusing bed:
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36. Refer to Exhibit 5A. If the amino acid glycine were placed in the bed where the pH is 7, and the current were turned on, it would migrate closest to which of the following positions?
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37. Refer to Exhibit 5A. If the amino acid glycine were placed in the bed where the pH is 11, and the current were turned on, it would migrate closest to which of the following positions?
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38. Refer to Exhibit 5A. A mixture of asp, asn, and arg is placed in the bed where the pH is 7, and the current is turned on. From left to right, which best represents the final positions of the individual amino acids?
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39. When electrophoretic separations are done based on molecular weight, the distance that a molecule moves can be graphed as a straight line when compared to:
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40. In electrophoresis experiments
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41. In isoelectric focusing gel electrophoresis
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42. The isoelectric point is
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43. Two dimensional separation methods
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44. Important steps in sequencing pure proteins include all of these except:
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45. If a protein with the sequence FEWPRQVDMARINE is treated with chymotrypsin, what will the products be?
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46. Which of the following treatments results in a polypeptide fragment with a homoserine lactone at the C-terminal end?
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47. If a protein with the sequence PQRKYPIG is treated with trypsin, what will the products be?
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48. Cyanogen bromide (CNBr) cleaves proteins
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49. It is impossible to sequence a protein if you do not have overlapping sequences to work with.
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50. The most efficient method for determining the sequence of a short peptide is:
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51. Methods for breaking proteins into smaller peptides include all of the following except:
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52. When end-group analysis was done on the protein insulin, the results indicated that both glycine and phenylalanine were N-terminal amino acids and both asparagine and alanine were C-terminal amino acids. These results indicate that
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53. Matrix-Assisted Laser Desorption Ionization is a type of _____ technique.
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54. An amino acid analyzer is an instrument used to determine
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55. Generally speaking, sequence techniques have become so sensitive that if you are able to isolate the protein on a gel, there is enough of it to get a significant amount of its sequence.
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56. Determination of the sequence of amino acids in a peptide is done by
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57. It is frequently possible to bypass the determination of the identity of the N-terminal amino acid of a protein because
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58. Which of the following is not used in protein structure determination?
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59. In an ELISA, the molecule that binds directly to the target protein is called the
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60. Which of the following explains why a secondary antibody is used in an ELISA?
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61. In an ELISA, the compound 4-chloro-1-naphthol is used because
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62. Which of the following is NOT true concerning a western blot?
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63. The purpose of using nitrocellulose for a western blot is to
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64. A protein chip is functionally most similar to which other technique?
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65. The most common way of visualizing the results seen on a protein chip is by use of
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66. Studying the entire complement of proteins being produced by a cell is called
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67. Studying how proteins interact with other proteins is called
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68. The process of breaking cells open to release the organelles is called _____.
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69. Which of the following polysaccharides is used to make up resins for use in electrophoresis and in column chromatography?
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| 70. What is the distinguishing feature of affinity chromatography?
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71. Which of the following is a similarity between ion-exchange chromatography and affinity chromatography?
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72. Identify a proteolytic enzyme that preferentially hydrolyzes amide bonds adjacent to aromatic amino acid residues.
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Original price was: $30.00.$20.00Current price is: $20.00.
Original price was: $30.00.$20.00Current price is: $20.00.
Original price was: $30.00.$20.00Current price is: $20.00.
Original price was: $30.00.$20.00Current price is: $20.00.
Original price was: $30.00.$20.00Current price is: $20.00.
Original price was: $30.00.$20.00Current price is: $20.00.
