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Urea has been widely used as a protein denaturant for more than a hundred years; however, its chemical denaturation mechanism still remains controversial, despite the extensive studies from both experimental and theoretical approaches in last several decades.1–19 The denaturing power of urea has been explained by two very different mechanisms: the “indirect” and “direct” mechanisms. The indirect mechanism suggests that urea denatures proteins by disrupting the water structure, which in turn weakens the hydrophobic interaction and makes the protein hydrophobic residues less compact and more readily solvated.4 The direct mechanism, on the other hand, indicates that urea unfolds proteins through direct interactions with protein, either through stronger electrostatic interactions10,11,13,16 with backbone and/or polar residues or through preferential van der Waals attractions14,15,18 with protein residues. Most of the concurrent studies support the direct mechanism involving urea's preferential binding to protein backbone or side chains,10,11,13–15,18 although some recent studies also indicate that the indirect mechanism can also play a role in the urea-induced protein denaturation.8,16,19

Comment on “Urea-Mediated Protein Denaturation: A Consensus View”