Question

question 3 of 15
what accounts for the finding that a protein functions normally in an aqueous buffer but loses its function when placed in an organic solvent such as hexane?
a. the protein loses its hydrophobic groups in an organic solvent.
b. the proteins overall shape can vary depending on the solvent.
c. the proteins primary sequence is altered in a new solvent.
d. the protein undergoes amino acid modification in an organic solvent.

Explanation:

Proteins' functions depend on their three - dimensional structure. Different solvents can affect this structure.

• Option A: Hydrophobic groups are part of the protein's structure and not lost in an organic solvent.
• Option B: The protein's shape (conformation) can change with the solvent. In an aqueous buffer, it has a native, functional shape. In an organic solvent like hexane, the non - polar environment disrupts the interactions (e.g., hydrogen bonds, hydrophobic interactions) that maintain its native shape, leading to loss of function.
• Option C: The primary sequence (amino acid sequence) is determined by genetics (DNA) and is not altered by the solvent.
• Option D: There is no amino acid modification just due to transfer to an organic solvent.

Answer:

B. The protein's overall shape can vary depending on the solvent.