Question

When Bs1A is assembled as an octamer, what is most likely to be true regarding L76, L77, and L79?

A. They are oriented toward the solvent-exposed exterior of the protein assembly.
B. The assembly would incur an entropic penalty if they occupied a solvent-exposed site.
C. Unlike in a monomer, they are not situated within the hydrophobic cap.
D. Their physiochemical properites are not substantially dependent on their hydrophobicity

Answer 1

When Bs1A is assembled as an octamer, L76, L77, and L79 are likely to be oriented toward the solvent-exposed exterior of the protein assembly.

Step-by-step explanation:

When the Bs1A protein is assembled as an octamer, it is most likely that L76, L77, and L79 are oriented toward the solvent-exposed exterior of the protein assembly (option A).

This is because solvent-exposed sites are more likely to have polar or charged amino acids, which L76, L77, and L79 are.

The assembly would incur an entropic penalty if these residues occupied a solvent-exposed site (option B), and unlike in a monomer, they are situated within the hydrophobic cap (option C).

Additionally, the physiochemical properties of these residues are substantially dependent on their hydrophobicity (option D).