word
Chaperone Proteins
SHAP-er-ohn PROH-teenz
/ˈʃæpəroʊn ˈproʊtiːnz/Listen
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Syllable breakdown
ChaperoneProteins
Dictionary meaning
A class of proteins that assist in the correct folding of newly synthesized or stress-denatured proteins, preventing inappropriate aggregation. Molecular chaperones, such as the Hsp70 and Hsp90 families, bind to exposed hydrophobic regions of unfolded proteins and provide a protected environment for proper refolding.
Examples
- Heat shock chaperone proteins are rapidly upregulated when cells are exposed to high temperatures.
- Without chaperone proteins, many newly made proteins would clump together before reaching their correct shape.
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