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 purpose of this review is to demonstrate the critical importance of understanding protein–
excipient interactions as a key step in the rational design of formulations to stabilize and …

Zwitterionic polymers exhibit excellent nonfouling performance due to their strong surface
hydrations. However, salt molecules may severely reduce the surface hydrations of typical …

Water is essential for life in many ways, and without it biomolecules might no longer truly be
biomolecules. In particular, water is important to the structure, stability, dynamics, and …

Molecular dynamics simulations of the protein chymotrypsin inhibitor 2 in 8 M urea at 60° C
were undertaken to investigate the molecular basis of chemical denaturation. The protein …

Vibrational sum-frequency generation (VSFG) spectroscopy is a powerful tool to study
interfaces. Recently, multiplex heterodyne-detected VSFG (HD-VSFG) has been developed …

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

Although it is widely known that trimethylamine N-oxide (TMAO), an osmolyte used by
nature, stabilizes the folded state of proteins, the underlying mechanism of action is not …

Lipid/water interfaces and associated interfacial water are vital for various biochemical
reactions, but the molecular-level understanding of their property is very limited. We …

The dynamics of water molecules next to hydrophobic solutes is investigated, specifically
addressing the recent controversy raised by the first time-resolved observations, which …