Hydrogen spectroscopy of

Simultaneous realisation of hydrogen charging or discharging process and in situ measurements of different NMR characteristic quantities give outstanding chances for the investigation and understanding of local physical properties of and hydrogen diffusion in disordered metal-hydrogen systems, including both equilibrium and non-equilibrium states. A few selected preliminary experimental results are presented in this letter for \ab{Pd_{0.9}Ag_{0.1}}-H alloy on in situ hydrogen concentration, proton NMR line-shift and magnetic susceptibility, {}^1{\ab H} NMR spectrum, spin-spin relaxation time and hydrogen diffusion activation energy and correlation time measurements. The motional averaged spectrum is asymmetric and the possible decompositions relate to the non-single-site residence of hydrogen in this alloy

Protein-Water and Protein-Buffer Interactions in the Aqueous Solution of an Intrinsically Unstructured Plant Dehydrin: NMR Intensity and DSC Aspects

Proton NMR intensity and differential scanning calorimetry measurements were carried out on an intrinsically unstructured late embryogenesis abundant protein, ERD10, the globular BSA, and various buffer solutions to characterize water and ion binding of proteins by this novel combination of experimental approaches. By quantifying the number of hydration water molecules, the results demonstrate the interaction between the protein and NaCl and between buffer and NaCl on a microscopic level. The findings overall provide direct evidence that the intrinsically unstructured ERD10 not only has a high hydration capacity but can also bind a large amount of charged solute ions. In accord, the dehydration stress function of this protein probably results from its simultaneous action of retaining water in the drying cells and preventing an adverse increase in ionic strength, thus countering deleterious effects such as protein denaturation