Reshaping the protein folding pathway by osmolyte via its effects on the folding intermediates.

Abstract

It is now well established that the protein folding reaction proceeds via accumulation of various intermediate states. Osmolytes, besides their role in protein stabilization, have also been shown to possess the ability of inducing tremendous affects on these protein folding intermediates, reshape the folding pathway and the energy landscape. The present article describes the advances made so far in understanding the effects of organic osmolytes on the folding intermediates and pathways. The ability of osmolytes to rescue disease causing mutations in proteins by inducing proper folding into functionally active form is also discussed. Finally, some future directions are described.