Difference between chaperones and chaperonins

Chaperones	Chaperonins
Small proteins	Large proteins
Assist in protein folding	Facilitate protein folding
Bind to exposed hydrophobic residues on unfolded proteins	Enclose the unfolded protein in a cavity
Prevent misfolding and aggregation of proteins	Provide a protected environment for the folding of proteins
Do not require ATP hydrolysis	Require ATP hydrolysis for their function
Examples include Hsp70 and Hsp90	Examples include GroEL and GroES

 

In summary, both chaperones and chaperonins are proteins that assist in protein folding, but they differ in their size, mechanism of action, and requirement for ATP hydrolysis. Chaperones are small proteins that bind to exposed hydrophobic residues on unfolded proteins and prevent misfolding and aggregation. Chaperonins, on the other hand, are large proteins that enclose the unfolded protein in a cavity and provide a protected environment for the folding of proteins. Chaperonins require ATP hydrolysis for their function, while chaperones do not. Examples of chaperones include Hsp70 and Hsp90, while examples of chaperonins include GroEL and GroES.