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Which consequence results when a protein's folding enthalpy is improperly minimized?

A)Aggregated structure and loss-of-function
B)Increased flexibility allows novel binding
C)Enhanced chaperone binding affinity results
D)Native folding is sped-up during refolding

💡 Explanation

Protein misfolding and aggregation occur because incorrect energy funnel landscapes associated with improper potential energy minimization cause hydrophobic domains to be exposed, therefore promoting intermolecular clumping, rather than forming the native structure.

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