Chaperone proteins play a role in
Protein folding
Protein misfolding
Denaturation
All the above
Chaperone proteins paicipate in the folding of over half of all mammalian proteins. They can "rescue" unfolded proteins that have become thermodynamically trapped in a misfolded dead end by unfolding hydrophobic regions and providing a second chance to fold productively. Ex: Glutathione can reduce inappropriate disulfide bonds that may be formed upon exposure to oxidizing agents such as O2, hydrogen peroxide, or superoxide Reference: Explanation: Harper's Biochemistry; 30th edition; Chapter 5; proteins: higher Orders of Structure
Structure and function of protein