Water structure around hydrophobic amino acid side chain analogs using different water models.

摘要: The water structure around hydrophobic groups governs various biochemical processes. There is an ongoing debate on whether molecules near are more ordered with greater participation in water-water hydrogen bonding respect to the pure bulk state. six different amino acid side chain analog has been studied using molecular dynamics simulations. analysis of tetrahedral order parameter and number bonds formed by individual first hydration shell analogs provide evidence that both ordering involving some extent reduced shell. It revealed tetrahedrality outer part equivalent for all models except TIP4P-2005 model which shows marginally higher tetrahedrality. However, irrespective employed, always found be inner shell, eventually makes overall lower than observed water. Importantly, it noticed decrease structuring exhibits solute size dependencies. Around a small like methane, or propensity quite similar effect, reduction structuring, however pronounced relatively larger solutes.