The structure and function of biomolecules are strongly influenced by their hydration shells.
Structural fluctuations and molecular excitations of hydrating water molecules cover a broad …

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

It has long been axiomatic that a protein's structure determines its function. Intrinsically
disordered proteins (IDPs) and disordered protein regions (IDRs) defy this structure …

Proteins exhibit structural fluctuations over decades of time scales. From the picosecond
side chain motions to aggregates that form over the course of minutes, characterizing protein …

Two-dimensional electronic spectroscopy (2DES) reveals connections between an optical
excitation at a given frequency and the signals it creates over a wide range of frequencies …

Macromolecular crowding is known to affect protein folding, binding of small molecules,
interaction with nucleic acids, enzymatic activity, protein-protein interactions, and protein …

The effects of crowding in biological environments on biomolecular structure, dynamics, and
function remain not well understood. Computer simulations of atomistic models of …

Membrane wetting by biomolecular condensates recently emerged as a key phenomenon in
cell biology, playing an important role in a diverse range of processes across different …

It is now generally accepted that macromolecules do not act in isolation but “live” in a
crowded environment, that is, an environment populated by numerous different molecules …

Infrared spectroscopy has played an instrumental role in the study of a wide variety of
biological questions. However, in many cases, it is impossible or difficult to rely on the …