Discussion
A mutation replaces a hydrophobic amino acid in the core of a protein with a hydrophilic one. What is the most likely consequence ?
Answer: B
The most likely consequence is disruption of protein folding.
A globular protein folds so that its hydrophobic side chains are buried in the core, away from water. This hydrophobic effect is one of the main forces holding the folded shape together. A hydrophilic or charged residue placed in the core cannot be shielded from water and cannot pack against its neighbours, so the core is destabilised and the protein tends to misfold or unfold.
'No change' ignores the hydrophobic effect. The protein becomes less stable, not more. Stronger ionic bonds are unlikely, because a lone polar group buried in a nonpolar core has no partner to bond with.
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