The option that is most likely to be true regarding L76, L77, and L79 is that option B: The assembly would incur an entropic penalty if they occupied a solvent-exposed site.
The entropic penalty in regards to ordered water is known to be one that tells or account for any form of weaker binding of the antibiotic novobiocin to what we call resistant mutant of DNA gyrase.
Note that in regards to the scenario above, the Entropic penalty is seen as the thermodynamically disfavored needs that is required in forming a cage of polar solvent molecules that is known to be seen around surface that has exposed hydrophobic potion of a molecule.
Hence, The option that is most likely to be true regarding L76, L77, and L79 is that option B: The assembly would incur an entropic penalty if they occupied a solvent-exposed site.
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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 properties are not substantially dependent on their hydrophobicity
