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.
Keywords: Folding kinetics, molten globule, native-like, osmolytes, protein folding, protein folding intermediates.
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