Ions differ in their ability to salt out proteins from solution as expressed in the lyotropic or
Hofmeister series of cations and anions. Since its first formulation in 1888, this series has …

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 …

Weakly hydrated anions help to solubilize hydrophobic macromolecules in aqueous
solutions, but small molecules comprising the same chemical constituents precipitate out …

The stability of proteins in aqueous solution is routinely enhanced by cosolvents such as
glycerol. Glycerol is known to shift the native protein ensemble to more compact states …

Accurate force fields are critical for meaningful simulation studies of highly concentrated
electrolytes. The ion models that are widely used in biomolecular simulations do not …

Currently, more than 100 isotherm models coexist for the six IUPAC isotherm types.
However, no mechanistic insights can be reached when several models, each claiming a …

The majority (∼ 70%) of surface buried in protein folding is hydrocarbon, whereas in DNA
helix formation, the majority (∼ 65%) of surface buried is relatively polar nitrogen and …

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

Salt-induced liquid–liquid phase separation in liquid mixtures is a common phenomenon in
nature and in various applications, such as in separation and extraction of chemicals. Here …

A comprehensive understanding of protein folding and biomolecular self-assembly in the
intracellular environment requires obtaining a microscopic view of the crowding effects. The …