Dynamics Of Water In Solutions Research Articles

Water dynamics in solutions of linear poly (N-isopropyl acrylamide) studied by 2H NMR field-cycling relaxometry

We use 2H nuclear magnetic resonance to study the dynamics of deuterated water in a solution of linear poly (N-isopropyl acrylamide) (pNIPAM, 4 wt%) across its coil-to-globule transition at a lower critical solubility temperature (LCST) around 32°C. In agreement with previous studies, we find that the 2H spin-lattice (T1) and, in particular, spin-spin (T2) relaxation times abruptly decrease when heating through the LCST, indicating that the polymer collapse causes an emergence of a water fraction with strongly reduced mobility. To quantify the dynamics of this slow water fraction, we exploit the fact that 2H field-cycling relaxometry allows us to measure the spectral density of the water reorientation in a broad frequency range. We find that the slow water fraction is characterised by a broad logarithmic Gaussian distribution of correlation times (σLG = 2.3), which is centred about τLG ≈ 10–9 s near the LCST. Hence, the common assumption of a Debye spectral density does not apply. We argue that a minor water fraction, which is located inside the pNIPAM globules and shows dynamics governed by the disordered polymer matrix, accompanies a major water fraction with bulk-like dynamics above the LCST. The former fraction amounts to about 0.4 water molecules per NIPAM monomer. Several findings indicate fast exchange between these bound and free water fractions on the T1 and T2 time scales.

Influence of ice formation on the dynamic and thermodynamic properties of aqueous solutions

Water dynamics in solutions with biological or non-biological solutes has been intensely studied when both components (solvent and solute) are amorphous. Here, we apply broadband dielectric spectroscopy combined with calorimetric measurements to analyze the dynamics of the aqueous solutions tri-propylene glycol (3PG) and ε-poly (lysine) (ε-PLL), after their water becomes semi-crystalline. Various crystallization levels were explored by conducting experiments with different annealing times at temperatures above the glass transition temperature (Tg). We find that the amount of ice depends on both the time and temperature of the annealing, and that this, in turn, affects Tg and dynamics of the amorphous part of the samples. However, it should be noted that the observed differences are relatively small for the degrees of crystallinity we have studied (up to about 26 wt% of the water). This also implies that the dynamic crossover of the water relaxation from a high temperature non-Arrhenius behavior to a low temperature Arrhenius dependence is unaffected by the partial crystallization and still occurs as a single crossover at the calorimetric Tg. Thus, we cannot detect two different crossovers, as commonly observed for other types of two-component systems, such as two glass formers.

Water dynamics in the hydration shells of biological and non-biological polymers.

The dynamics of water at supercooled temperatures in aqueous solutions of different types of solutes has been deeply analyzed in the literature. In these previous works and in most of the cases, a single relaxation of water molecules is observed. In this work, we analyze the dynamics of water in solutions for which a dual relaxation of water molecules is experimentally measured. We discuss the criteria for observing these two water relaxations in these specific solutions and their most likely origins. We also discuss how these two water relaxations relate to the relaxation behavior of bulk water and how the slower one is coupled to the solute dynamics and is essential for the dynamics and functional properties of proteins.

Observation of Water Separated Ion-Pairs between Cations and Phospholipid Headgroups

In this work, we present evidence for ion pair formation of cations with a high surface charge density (Na(+) and Ca(2+)) and phosphate groups of phospholipids. We used femto-second infrared pump-probe and dielectric spectroscopy to probe the dynamics of water molecules in solutions of phosphorylethanolamine and different types of cations. We find that sodium and calcium cooperatively retard the dynamics of water in solutions of phosphorylethanolamine, implying the formation of solvent separated ion pairs. This ion-specific interaction is absent for potassium, cesium and ammonium. We compare our results to dielectric spectroscopy experiments, which probes the rotation of all dipolar molecules and ions in solution. The rotation of the dipolar phosphorylethanolamine ion shows that long-lived ion-pairs are only formed with calcium and not with ammonium, cesium, potassium, and sodium. This finding implies that the association between calcium and the phosphate is strong with lifetimes exceeding 200 ps, while the interaction with sodium is relatively short-lived (∼20-100 ps).

Femtosecond study of the effects of ions and hydrophobes on the dynamics of water

We study the effects of ions and hydrophobic molecular groups on the orientational dynamics of water using THz dielectric relaxation (THz-DR) and polarization-resolved femtosecond infrared (fs-IR) pump-probe spectroscopy. We measure the dynamics of water in solutions of NaI, NaCl, CsCl, guanidinium chloride (GndCl) and tetramethyl guanidinium chloride (TMGndCl) of different the static dipoles of their surrounding water molecules. With fs-IR we find that concentrations. With THz-DR we observe that strongly hydrated cations align the OD groups that form hydrogen bonds to halide anions reorient with two distinct time constants of 2 +/- 0.3 ps and 9 +/- 1 ps. The fast process is assigned to a wobbling motion of the OD group that keeps the hydrogen bond with the anion intact. The amplitude of this wobbling motion depends on the nature of both the anion and the counter cation. The replacement of four of the six hydrogen atoms of the weakly hydrated cation guanidinium by hydrophobic methyl groups leads to an exceptionally strong slowing down of the water dynamics. Hydrophobic groups thus appear to have a much stronger effect on the dynamics of water than ions. These findings give new insights in the mechanism of protein denaturation by GndCl and TMGndCl.

Universal features of water dynamics in solutions of hydrophilic polymers, biopolymers, and small glass-forming materials

A systematic investigation by dielectric spectroscopy of 18 different water-rich mixtures with very different hydrophilic substances shows universal features for the water dynamics. The temperature dependence of the relaxation times exhibits a crossover from non-Arrhenius to Arrhenius behavior at the T(g) range of the mixtures. Furthermore, the temperature dependence of the relaxation times presents a universal behavior both above and below the crossover temperature. We also show that these features suggest that the observed crossover is associated with the emergence of confinement effects.

Single particle and collective hydration dynamics for hydrophobic and hydrophilic peptides

We have conducted extensive molecular dynamics simulations to study the single particle and collective dynamics of water in solutions of N-acetyl-glycine-methylamide, a model hydrophilic protein backbone, and N-acetyl-leucine-methylamide, a model (amphiphilic) hydrophobic peptide, as a function of peptide concentration. Various analytical models commonly used in the analysis of incoherent quasielastic neutron scattering (QENS), are tested against the translational and rotational intermediate scattering function, the mean square displacement of the water molecule center of mass, and fits to the second-order rotational correlation function of water evaluated directly from the simulation data. We find that while the agreement between the model-free analysis and analytical QENS models is quantitatively poor, the qualitative feature of dynamical heterogeneity due to caging is captured well by all approaches. The center of mass collective and single particle intermediate scattering functions of water calculated for these peptide solutions show that the crossover from collective to single particle-dominated motions occurs at a higher value of Q for high concentration solutions relative to low concentration because of the greater restriction in movement of water molecules due to confinement. Finally, we have shown that at the same level of confinement of the two peptides, the aqueous amphiphilic amino acid solution shows the strongest deviation between single particle and collective dynamics relative to the hydrophilic amino acid, indicating that chemical heterogeneity induces even greater spatial heterogeneity in the water dynamics.