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Which consequence inhibits protein misfolding when chaperone proteins deplete ATP?

A)Decreased hydrophobic surface interactions
B)Increased disulfide bond formation
C)Elevated proteasome enzymatic activity
D)Enhanced unfolded protein degradation

💡 Explanation

Decreased hydrophobic surface interactions occur as the exposure reduces when ATP depletion impairs chaperone protein function, leading to hampered folding and aggregation because this disrupts hydrophobic collapse. Therefore, the outcome changes, rather than efficient protein processing under normal conditions.

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