Water is an essential participant in the stability, structure, dynamics, and function of proteins
and other biomolecules. Thermodynamically, changes in the aqueous environment affect …

Elucidating the details of the formation, stability, interactions, and reactivity of biomolecular
systems under extreme environmental conditions, including high salt concentrations in …

The recent availability of long equilibrium simulations of protein folding in atomistic detail for
more than 10 proteins allows us to identify the key interactions driving folding. We find that …

Liquid–liquid phase separation (LLPS) of proteins and other biomolecules play a critical role
in the organization of extracellular materials and membrane‐less compartmentalization of …

The extent of the effect of cellular crowding and cosolutes on the functioning of proteins and
cells is manifold and includes the stabilization of the biomolecular systems, the excluded …

High hydrostatic pressure affects the structure, dynamics, and stability of biomolecular
systems and is a key parameter in the context of the exploration of the origin and the …

Accurate force fields are one of the major pillars on which successful molecular dynamics
simulations of complex biomolecular processes rest. They have been optimized for ambient …

Now that the centennial anniversary of the first report on pressure denaturation of proteins
by Nobel Laureate PW Bridgman can be celebrated, this Review on the application of high …

Fast-folding proteins have been a major focus of computational and experimental study
because they are accessible to both techniques: they are small and fast enough to be …

Investigating the kinetics of biochemical reactions plays vital roles in understanding the
reaction mechanism. However, many biochemical reactions occur in the time scale of …