Nature achieves differentiation of specific and nonspecific binding in molecular interactions
through precise control of biomolecules in space and time. Artificial systems such as …

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

Protein–protein association is fundamental to many life processes. However, a microscopic
model describing the structures and kinetics during association and dissociation is lacking …

Traditional descriptions of the hydrophobic effect on the basis of entropic arguments or the
calculation of solvent‐occupied surfaces must be questioned in view of new results obtained …

Interactions between proteins are orchestrated in a precise and time-dependent manner,
underlying cellular function. The binding affinity, defined as the strength of these …

Protein–protein interactions form central elements of almost all cellular processes.
Knowledge of the structure of protein–protein complexes but also of the binding affinity is of …

Protein-based bioactive coatings have emerged as a versatile and promising strategy for
enhancing the performance and biocompatibility of diverse biomedical materials and …

Despite the biological importance of protein–protein complexes, determining their structures
and association mechanisms remains an outstanding challenge. Here, we report the results …

New molecular modeling approaches, driven by rapidly improving computational platforms,
have allowed many success stories for the use of computer-assisted drug design in the …

Dielectric permittivity is central to many biological and physiochemical systems, as it affects
the long-range electrostatic interactions. Similar to many fluid properties, confinement …