Chaperones

Definition

Chaperones are proteins that assist in the proper folding of other proteins and prevent misfolding. They play a critical role in maintaining cellular homeostasis and protein quality control.

5 Must Know Facts For Your Next Test

1. Chaperones bind to nascent or unfolded polypeptides to prevent incorrect folding.
2. Heat shock proteins (HSPs) are a major class of chaperones upregulated in response to stress.
3. Chaperonins, such as GroEL/GroES in bacteria, provide an isolated environment for protein folding.
4. Molecular chaperones can recognize exposed hydrophobic regions on misfolded proteins.
5. ATP hydrolysis is often required for the function of many chaperone proteins.

Review Questions

• What is the primary function of chaperone proteins?
• How do heat shock proteins relate to chaperones?
• Why is ATP important for the function of many chaperone proteins?

Related terms

Heat Shock Proteins (HSPs): A family of chaperones that are upregulated during cellular stress.

Chaperonin: A type of chaperone that provides a protected environment for protein folding.

Protein Misfolding: A process where proteins fail to fold into their correct functional conformations.