Chemical denaturants inhibit the onset of dewetting.
The mechanism by which the aqueous cosolvents guanidinium chloride and urea denature proteins is a matter of controversy. Here, we use all-atom molecular dynamics simulations to study the effect of both denaturants on the dewetting of water confined between nanoseparated hydrophobic plates. It is found that the denaturants inhibit the onset of dewetting, so that it occurs at shorter interplate distances than in pure water. Our results support a role for urea and guanidinium in assisting in the solvation of nonpolar surfaces, thereby weakening hydrophobic effects known to be important for protein stability.
England
Jeremy L
JL
Department of Physics, Stanford University, Stanford California 94305, USA.
Pande
Vijay S
VS
Haran
Gilad
G
D019791:Guanidine / Q000737:chemistry*; D057927:Hydrophobic and Hydrophilic Interactions; D008958:Models, Molecular; D011489:Protein Denaturation; D012996:Solutions; D014508:Urea / Q000737:chemistry*; D014867:Water / Q000737:chemistry*; D017155:Wettability
D012996:Solutions; D014867:Water; D014508:Urea; D019791:Guanidine