The biological activity of proteins depends on their three-dimensional structure, known as
the native state. The main force driving the correct folding mechanism is the hydrophobic …

In the past decade, many gas-phase spectroscopic investigations have focused on the
understanding of the nature of weak interactions in model systems. Despite the fact that non …

We use 1H NMR to probe the energy landscape in the protein folding and unfolding
process. Using the scheme⇄ reversible unfolded (intermediate)→ irreversible unfolded …

The role the solvent plays in determining the biological activity of proteins is of primary
importance. Water is the solvent of life and proteins need at least a water monolayer …

Functional monomers in dentin adhesives are involved in wetting dental substrates,
demineralization, and the formation of calcium salts. However, the interaction of these …

We have investigated the nuclear spin relaxation properties of 1H in liquid water with the
help of molecular dynamics simulations. We have computed the 1H nuclear spin relaxation …

The thermodynamic response functions of water display anomalous behaviors. We study
these anomalous behaviors in bulk and confined water. We use nuclear magnetic …

Protein unfolding occurs at both low and high temperatures, although in most cases, only the
high-temperature transition can be experimentally studied. A pressing question is how much …

Optimization procedures for industrial spray drying processes mainly rely on empirical
understanding. Mechanistic understanding of the process is limited, but can be enhanced by …

Ion-specific effects at the protein surface are investigated here in light of the changes they
infer to surface water dynamics, as observed by 1H NMR relaxation (at 20 MHz). Two well …