By confining water in a nanoporous structure so narrow that the liquid could not freeze, it is possible to study properties of this previously undescribed system well below its homogeneous nucleation temperature T _H = 231 K. Using this trick, we were able to study, by means of a Fourier transform infrared spectroscopy, vibrational spectra (HOH bending and OH-stretching modes) of deeply supercooled water in the temperature range 183 < T < 273 K. We observed, upon decreasing temperature, the building up of a new population of hydrogen-bonded oscillators centered around 3,120 cm ⁻¹ , the contribution of which progressively dominates the spectra as one enters into the deeply supercooled regime. We determined that the fractional weight of this spectral component reaches 50% just at the temperature, T _L ≈ 225 K, where the confined water shows a fragile-to-strong dynamic cross-over phenomenon [Ito, K., Moynihan, C. T., Angell, C. A. (1999) Nature 398:492–494]. Furthermore, the fact that the corresponding OH stretching spectral peak position of the low-density-amorphous solid water occurs exactly at 3,120 cm ⁻¹ [Sivakumar, T. C., Rice, S. A., Sceats, M. G. (1978) J. Chem. Phys. 69:3468–3476.] strongly suggests that these oscillators originate from existence of the low-density-liquid phase derived from the occurrence of the first-order liquid–liquid (LL) phase transition and the associated LL critical point in supercooled water proposed earlier by a computer molecular dynamics simulation [Poole, P. H., Sciortino, F., Essmann, U., Stanley, H. E. (1992) Nature 360:324–328].

We study the dynamics of hydration water in the protein lysozyme in the temperature range 180K<T<360K using Fourier-transform-infrared and nuclear magnetic resonance (NMR) spectroscopies. By analyzing the thermal evolution of spectra of the OH-stretching vibration modes and the NMR self-diffusion (DS) and spin-lattice relaxation time (T1), we demonstrate the existence of two dynamical transitions in the protein hydration water. Below the first transition, at about 220K, the hydration water displays an unambiguous fragile-to-strong dynamic crossover, resulting in the loss of the protein conformational flexibility. Above the second transition, at about 346K, where the protein unfolds, the dynamics of the hydration water appears to be dominated by the non-hydrogen-bonded fraction of water molecules.

Invertebrates represent the most plentiful component of marine biodiversity. To date, only few species have been documented for marine litter intake. Here, we report for the first time the presence of macroplastic debris in a jellyfish species. Such novel target to plastic pollution highlights an under studied vector of marine litter along marine trophic web, raising further concern over the impact on marine wildlife.