# Explain how chaperone proteins assist in the correct folding of newly synthesised polypeptides.

> IB DP Biology Higher Level (2023 syllabus) — B1.2 Proteins · Explain · 4 marks

## Mark scheme (4 marks)

1. Newly synthesised polypeptides emerging from ribosomes are at risk of misfolding or forming incorrect interactions with other polypeptides / aggregating.
2. Chaperone proteins bind to exposed hydrophobic regions of the unfolded/partially folded polypeptide, preventing premature or incorrect interactions.
3. Chaperones use energy from ATP hydrolysis to drive conformational changes that release the polypeptide, allowing it to fold correctly.
4. The process may be repeated (iterative cycles of binding and release) until the polypeptide achieves its stable, correctly folded tertiary/quaternary structure.

## Key terms

- [chaperone protein](https://www.gradenine.co.uk/glossary/chaperone-protein)

## Related

- [Revision notes for IB DP Biology Higher Level (2023 syllabus)](https://www.gradenine.co.uk/learn)
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Source: [GradeNine](https://www.gradenine.co.uk/q/explain-how-chaperone-proteins-assist-in-8e57cc5e) · Published by Druglandscape Ltd.