In an aqueous solution, protein conformation is determined by two major factors.

Q: In an aqueous solution, protein conformation is determined by two major factors.

61. The correct answer is an option D, i.e. placement of hydrophobic amino residues within the interior of the protein. 62. The correct answer is an option E, i.e. they may retain their correct shape even when separated from the rest of the protein. 63. The correct answer is an option E, i.e. iodoacetic acid.

ID: 543849 • Letter: I

Question

In an aqueous solution, protein conformation is determined by two major factors. One is the maintenance of the maximum number of hydrogen bonds. The 64. Addition of a trace amount of chaperone to a protein denaturation experiment Will shift the curve to the right, less denaturant required to unfold the protein Will shift the curve to the left, more denaturant required to unfold the protein Will not change the shape or position of the denaturation curve May allow for faster equilibration of the folded and unfolded species A. other is the: A. formation of the maximum number of hydrophilic interactions. maximization of ionic interactions. minimization of entropy by the formation of a water solvent shell around the protein. placement of hydrophobic amino acid residues within the interior of the protein. placement of polar amino acid residues around the exterior of the protein. B. B. C. C. D. E. Cand D D. 65. A prosthetic group of a protein is a non- E. protein structure that is: transiently bound to the protein. permanently associated with the protein. a substrate of the protein. a part of the secondary structure of the protein. a ligand of the protein. A. B. 2. Which of the following statements concerning protein domains is true? They are a form of secondary structure. C. D. A. B. C. D. E. They are examples of structural E. 66. In the binding of oxygen to myoglobin, the They consist of separate polypeptide chains (subunits). They have been found only in prokaryotic proteins. They may retain their correct shape even when separated from the rest of the protein. relationship between the concentration of oxygen and the fraction of binding sites occupied can best be described as: A. B. C. D. E. sigmoidal random. linear with a positive slope. linear with a negative slope. hyperbolic. 53. An average protein will not be denatured by: A. a detergent such as sodium dodecyl B. heating to 90°C C. iodoacetie acid. (Alkylates Sulfhydrils) D. pH 10 E. urea.

Explanation / Answer

61. The correct answer is an option D, i.e. placement of hydrophobic amino residues within the interior of the protein.

62. The correct answer is an option E, i.e. they may retain their correct shape even when separated from the rest of the protein.

63. The correct answer is an option E, i.e. iodoacetic acid.

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In an aqueous solution, protein conformation is determined by two major factors.

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