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 …

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

Trimethylamine N-oxide (TMAO) is a naturally occurring protecting osmolyte that stabilizes
the folded state of proteins and also counteracts the destabilizing effect of urea on protein …

Cosolvents modulate aqueous solubility, hydrophobic interactions, and the stability and
function of most proteins in the living cell. Our molecular-level understanding of cosolvent …

Chemical denaturants are the most commonly used agents for unfolding proteins and are
thought to act by better solvating the unfolded state. Improved solvation is expected to lead …

Using molecular dynamics (MD) simulations in conjunction with the SPC/E water model, we
optimize ionic force-field parameters for seven different halide and alkali ions, considering a …

Drugs that are poorly soluble in water can be solubilized by the addition of hydrotropes.
Albeit known for almost a century, how they work at a molecular basis is still controversial …

Ionic liquids (ILs) are used in a variety of technological and biological applications. Recent
experimental and simulation results reveal the influence of aqueous ionic liquids on the …

An aqueous solution of urea is a very important mixture of biological relevance because of
the definitive role of urea as protein denaturant at high concentrations. There has been an …

In aqueous solutions with high concentrations of chemical denaturants such as urea and
guanidinium chloride (GdmCl) proteins expand to populate heterogeneous conformational …