We present an overview of recent static and time-resolved vibrational spectroscopic studies
of liquid water from ambient conditions to the supercooled state, as well as of crystalline and …

Proteins are marginally stable, and the folding/unfolding equilibrium of proteins in aqueous
solution can easily be altered by the addition of small organic molecules known as …

The interior of the cell is a densely crowded environment in which protein stability is affected
differently than in dilute solution. Macromolecular crowding is commonly understood in …

We report experimental and computational studies investigating the effects of three
osmolytes, trimethylamine N-oxide (TMAO), betaine, and glycine, on the hydrophobic …

While the development of weakly coordinating anions (WCAs) received much attention, the
progress on weakly coordinating and inert solvents almost stagnated. Here we study the …

Develo** efficient polymeric membranes for the purification of emulsified oily wastewater
is of great significance but still challenging, restricted by low flux and severe membrane …

There is a long, ongoing debate on how small molecules (osmolytes) affect the stability of
proteins. The present study found that change in collective rotational dynamics of water in …

Osmolytes are essential for cellular function under ubiquitous osmotic stress.
Trimethylamine N-oxide (TMAO) is one such osmolyte that has gained remarkable attention …

The free energy and conformational landscape of biomolecular systems as well as
biochemical reactions depend not only on temperature and pressure, but also on the …

The mechanism of protein stabilization by osmolytes remains one of the most important and
long-standing puzzles. The traditional explanation of osmolyte-induced stability through the …