In an aqueous solution, protein conformation is determined by two major factors. One is the maintenance of the maximum number of hydrogen bonds. The other is the: Addition of a trace amount of chaperone to a protein denaturation experiment 64. A. Will shift the curve to the right, less denaturant required to unfold the formation of the maximum number of hydrophilic interactions. A. Will shift the curve to the left, more denaturant required to unfold the B. B. maximization of ionic interactions C. minimization of entropy by the C. Will not change the shape or 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 position of the denaturation curve D. May allow for faster equilibration D. of the folded and unfolded species E. Cand D 65. A prosthetic group of a protein is a non- E. protein structure that is: A. B. transiently bound to the protein. permanently associated with the 2. Which of the following statements concerning protein domains is true? C. D. a substrate of the protein. A. They are a form of secondary B. They C. They consist of separate D. E. a part of the secondary structure of the protein are examples of structural a ligand of the protein. 66. In the binding of oxygen to myoglobin, the E. motifs. relationship between the concentration of 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. 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. 3. An average protein will not be denatured A. a detergent such as sodium dodecyl sulfate. B. heating to 90°C. C. iodoacetic acid. (Alkylates Sulfhydrils) D. pH 10. E. urea.