  Numerical simulations of hydrated proteins show that protein hydration shells
are polarized into a ferroelectric cluster with a large magnitude of its
average dipole moment. The emergence of this new mesophase dramatically alters
the statistics of electrostatic fluctuations at the protein/water interface.
The linear-response relation between the average electrostatic potential and
its variance breaks down, with the breadth of the electrostatic noise far
exceeding the expectations of the linear response theories. The dynamics of
these non-Gaussian electrostatic fluctuations are dominated by a slow (~ 1 ns)
component which freezes in at the temperature of dynamical transition of
proteins.
