▪ Abstract Heat capacity (Cp) is one of several major thermodynamic quantities commonly
measured in proteins. With more than half a dozen definitions, it is the hardest of these …

The effect of cosolvents on biomolecular equilibria has traditionally been rationalized using
simple binding models. More recently, a renewed interest in the use of Kirkwood–Buff (KB) …

Rapid dissolution of cellulose in LiOH/urea and NaOH/urea aqueous solutions was studied
systematically. The dissolution behavior and solubility of cellulose were evaluated by using …

Cellulose can be dissolved in precooled (− 12° C) 7 wt% NaOH− 12 wt% urea aqueous
solution within 2 min. This interesting process, to our knowledge, represents the most rapid …

Neutron diffraction experiments were carried out on aqueous solutions containing either
guanidinium or thiocyanate ions. The first-order difference method of neutron diffraction and …

Classical molecular dynamics simulations were performed to investigate the effects of salt
on the lower critical solution temperature (LCST) of Poly (N-isopropylacrylamide)(PNIPAM) …

In order to clarify the mechanism of denaturant-induced unfolding of proteins we have
calculated the interactions between hydrophobic and ionic species in aqueous guanidinium …

Vibrational sum frequency spectroscopy was used to probe fatty amine monolayers spread
on various electrolyte solutions. The spectra revealed ion specific changes in both …

It is of great interest to determine how solutes such as urea, sugars, guanidinium salts, and
trimethylamine N-oxide affect the stability, solubility, and solvation of globular proteins. A key …

In the current work, an experimental and theoretical study is performed on the urea-water
mixtures by using non-covalent interactions (NCI) and reduced density gradient (RDG) …