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Elucidation of possible pathways between folded (native) and unfolded statesof a protein is a challenging task, as the intermediates are often hard todetect. Here we alter the solvent environment in a controlled manner bychoosing two different co-solvents of water, urea and dimethyl sulphoxide(DMSO), and study unfolding of four different proteins to understand therespective sequence of melting by computer simulation methods. We indeed findinteresting differences in the sequence of melting of alpha-helices andbeta-sheets in these two solvents. For example, at 8M urea solution, beta-sheetparts of a protein is found to unfold preferentially, followed by the unfoldingof alpha helices. In contrast, 8M DMSO solution unfolds alpha helices first,followed by the separation of beta-sheets for majority of proteins. Sequence ofunfolding events in four different alpha/beta proteins and also in chickenvillin head piece (HP-36) both in urea and DMSO solution demonstrate that theunfolding pathways are determined jointly by relative exposure of polar andnon-polar residues of a protein and the mode of molecular action of a solventon that protein.

A Comparative Study of Protein Unfolding in Aqueous Urea and DMSO  Solutions: Surface Polarity, Solvent Specificity and Sequence of Secondary  Structure Melting