Introduction to Molecular Chaperones and Their Functions

A set of flashcards covering key vocabulary and concepts related to molecular chaperones, their functions, and mechanisms.

Molecular Chaperones

Proteins that assist other proteins in folding and assembly.

Heat Shock Proteins (HSPs)

A group of proteins that are expressed in response to stress and help in protein folding, e.g., HSP70, HSP90, HSP100.

Protein Homeostasis

The maintenance of proper protein folding and assembly, vital for cell function.

Chaperone Network

The interconnected system of molecular chaperones that work together to assist with protein folding.

Hydrophobic Residues

Amino acids that do not interact well with water, needing to be packed into the core during protein folding.

ATP-Dependent Chaperones

Chaperones that require ATP energy to assist in protein folding, such as Hsp70, Hsp60 (GroEL), and Hsp90.

Non-Native Interactions

Incorrect interactions between amino acids that can cause protein folding to stall.

Prefoldin

A hetero-hexameric molecular chaperone involved in preventing aggregation and facilitating proper protein folding.

Calnexin and Calreticulin

ATP-independent chaperones that catalyze disulfide bond rearrangements during protein folding.

Co-Chaperones

Proteins that assist chaperones in their function, influencing their activity and client protein delivery.