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Urea denatures proteins due to its strong tendency to dehydrate the firstsolvation shell via urea-residue preferential binding. However, even afterextensive experimental and computational investigations, the influence of ureaon the stability of secondary structures remains elusive. For example, contraryto the common understanding, experimental studies have indicated that specificpolypeptides, such as poly-alanine or alanine-rich systems, may even show animproved tendency to form secondary structures in aqueous urea. We investigatethis seemingly counter-intuitive behaviour using over 15$\mu$s long all-atomsimulations. These results show how a delicate balance between the localizeddipole orientations and hydrogen bonding dictates polypeptide solvation inaqueous urea. Our work establishes a structure-property relationship thathighlights the importance of microscopic dipole-dipoleorientations/interactions for the operational understanding of macroscopicprotein solvation.

Stabilizing $\alpha-$helicity of polypeptide in aqueous urea: Dipole orientation or hydrogen bonding?