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Which outcome occurs when a protein misfolds during molecular assembly inside a chaperone protein complex?

A)Ubiquitination and proteasomal degradation
B)Immediate refolding without energy input
C)Stabilization via disulfide bond formation
D)Aggregation into functional amyloid fibrils

💡 Explanation

When a protein misfolds within a chaperone, exposed hydrophobic regions trigger ubiquitination because cellular quality control pathways mark it for degradation by the proteasome. Therefore, ubiquitination occurs, rather than immediate refolding, stabilization, or amyloid formation, which require specific conditions or structural features.

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