Question

1. (a) How do Chaperones prevent aggregation?

(b) Is the existence of chaperons, and their necessity in many cases, consistent with the idea that ALL of the folding information for proteins is in the primary sequence?

(c) Reconcile (or refute) the fact that chaperonins require ATP energy for their activity with the statement that proteins "self-assemble".

Answer 1

A) chaperons In the cell involve in folding and unfolding of protein as well as assembly and in disassembly.

They function as a foldable. Under condition of heat shock that is incress temperature. There synthesis is increased in the cell

They bind with the proteins and prevent their disassembly and further aggregation. Eg Hsp33 and DnJ proteins.

While some chaperones assist in protein during their folding.

B) all the information required for protein function and its conformation resides in the primary structure of protein itself.

Chaperons bind with newly synthsized protein hydrophobic part and assist in their folding. They them selves do not have information for protein folding.

C) proteins are self assembled in nature but chaperons bind to protein assist in the folding. Binding of chaperons require ATP , and assisting in change in conformation of protein during folding also requires ATP .