|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.