Pressure Effects in Supercooled Water: Comparison between a 2D Model of Water and Experiments for Surface Water on a Protein

TL;DR

This study compares a 2D water model's predictions with experiments on surface water near proteins, confirming pressure-dependent dynamic crossover behaviors and phase coexistence in supercooled water.

Contribution

It validates theoretical predictions about water's dynamic crossover and phase behavior using experimental data on protein surfaces, linking models with real-world observations.

Findings

Dynamic crossover is pressure-independent in time.

Activation energy decreases with increasing pressure.

Crossover temperature decreases as pressure increases.

Abstract

Experiments in bulk water confirm the existence of two local arrangements of water molecules with different densities, but, because of inevitable freezing at low temperature $T$, can not ascertain whether the two arrangements separate in two phases. To avoid the freezing, new experiments measure the dynamics of water at low $T$ on the surface of proteins, finding a crossover from a non-Arrhenius regime at high $T$ to a regime that is approximately Arrhenius at low $T$. Motivated by these experiments, Kumar et al. [Phys. Rev. Lett. 100, 105701 (2008)] investigated, by Monte Carlo simulations and mean field calculations, the relation of the dynamic crossover with the coexistence of two liquid phases in a cell model for water and predict that: (i) the dynamic crossover is isochronic, i.e. the value of the crossover time $\tau_{\rm L}$ is approximately independent of pressure $P$; (ii) the Arrhenius activation energy $E_{\rm A}(P)$ of the low-$T$ regime decreases upon increasing $P$; (iii) the temperature $T^*(P)$ at which $\tau$ reaches a fixed macroscopic time $\tau^*\geq \tau_{\rm L}$ decreases upon increasing $P$; in particular, this is true also for the crossover temperature $T_{\rm L}(P)$ at which $\tau=\tau_{\rm L}$. Here, we compare these predictions with recent quasi elastic neutron scattering (QENS) experiments performed by X.-Q. Chu {\it et al.} on hydrated proteins at different values of $P$. We find that the experiments are consistent with these three predictions.