Investigating protein–protein interactions is crucial for understanding cellular biological
processes because proteins often function within molecular complexes rather than in …

Cells are crowded, but proteins are almost always studied in dilute aqueous buffer. We
review the experimental evidence that crowding affects the equilibrium thermodynamics of …

Biological macromolecules function in highly crowded cellular environments. The structure
and dynamics of proteins and nucleic acids are well characterized in vitro, but in vivo …

We develop a detailed description of protein translational and rotational diffusion in
concentrated solution on the basis of all-atom molecular dynamics simulations in explicit …

It is currently unclear how the crowded cellular milieu affects the structural distributions of
intrinsically disordered proteins (IDPs). Here we employ single-molecule Förster resonance …

Intrinsically disordered proteins (IDPs) abound in cellular regulation. Their interactions are
often transitory and highly sensitive to salt concentration and posttranslational modifications …

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

Proteins in the cellular milieu reside in environments crowded by macromolecules and other
solutes. Although crowding can significantly impact the protein folded state stability, most …

The cellular interior is composed of a variety of microenvironments defined by distinct local
compositions and composition-dependent intermolecular interactions. We review the …

Biomolecules evolve and function in densely crowded and highly heterogeneous cellular
environments. Such conditions are often mimicked in the test tube by the addition of artificial …