Question

Compare and contrast the different classes of molecular chaperones

Answer 1

Answer:

The proteins that can assist the covalent folding or unfolding and Assembly or disassembly of other macro molecular structures.

These are having different families. Each familty aid to protein folding in different way.

Hsp60:

It is the large chaperon complex and it is so large it can accommodate native folding of 54-kDa GFP in its lumen.It acts a molecular chaperon in Mitochondrial matrix.

Hsp70:

It is the small chaperon and which increases the ATP consuption rate. This chaperon also decreases the tendency of opoptosis.

Hsp90:

It is the less understood chaperon. Its necessary for viability in eukaryotes and essential for activating many signaling proteins in the eukaryotic cell.

It cooperates with the Hsp70 chaperone system.

Hsp100:

The proteins have been studied in vivo and in vitro for their ability to target and unfold tagged and misfolded proteins.

Some of these Hsp100 chaperones like ClpA and ClpX are associate with the double-ringed tetradecameric serine protease ClpP instead of catalyzing the refolding of client proteins, These complexes are responsible for the targeted destruction of tagged and misfolded proteins.