Helén Jansson

TL;DR: It is shown here that the dominant conformational motions are slaved by the hydration shell and the bulk solvent, and the model quantitatively predicts the rapid increase of the mean-square displacement above ≈200 K and explains the nonexponential time dependence of the protein relaxation after photodissociation.

TL;DR: It is shown that the viscosity-related main (alpha) relaxation of confined water vanishes at a temperature where the volume required for the cooperative alpha relaxation becomes larger than the size of the geometrically confined water cluster, implying that above this temperature the authors observe a merged alpha-beta relaxation, whereas below it only a local (beta) relaxation remains.

TL;DR: This study uses differential scanning calorimetry (DSC) and viscometry measurements to determine how the glass transition temperature Tg, the protein denaturation temperature Tden, and the dynamic viscosity depend on both the trehalose and the protein concentration in myoglobin-trehalose-water systems.

TL;DR: For all samples it is clear that several proteins processes are involved in the calorimetric glass transition and the broadness of the transition depends on how much these different relaxations are separated in time.

TL;DR: In this article, the role of hydration water for protein dynamics was studied by broadband dielectric spectroscopy with the aim to understand the role in protein dynamics, showing Arrhenius temperature dependences, showing that at low temperatures (below approximately 200 K) confined water generally exhibits two relaxation processes: one process that is due to the local β-relaxation, and a faster and even more local process from the motion of Bjerrum-type defects.