Chaperone proteins play a role in

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