Which mechanism inhibits peptide folding accuracy during translation in a ribosome lacking chaperone proteins?

💡 Explanation

When chaperone proteins are absent, nascent polypeptide chains misfold because there's no assistance to properly form hydrogen bonds which stabilize correct secondary structures, leading to incorrect folding pathways. Therefore misfolding results, rather than hydrophobic collapse alone, disulfide bond errors, or aggregation which happen in different context.

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