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 …

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

Despite increased attention, little is known about how the crowded intracellular environment
affects basic phenomena like protein diffusion. Here, we use NMR to quantify the rotational …

There is abundant, physiologically relevant knowledge about protein cores; they are
hydrophobic, exquisitely well packed, and nearly all hydrogen bonds are satisfied. An …

Nuclear pore complexes (NPCs) form a selective filter that allows the rapid passage of
transport factors (TFs) and their cargoes across the nuclear envelope, while blocking the …

Although overexpression and 15N enrichment facilitate the observation of resonances from
disordered proteins in Escherichia coli, 15N enrichment alone is insufficient for detecting …

Proteins are essential and abundant components of cellular membranes. Being densely
packed within the limited surface area, proteins fulfil essential tasks for life, which include …

For a long time, the effect of a crowded cellular environment on protein dynamics has been
largely ignored. Recent experiments indicate that proteins diffuse more slowly in a living cell …

It is hard to imagine a more extreme contrast than that between the dilute solutions used for
in vitro studies of protein folding and the crowded, compartmentalized, sticky, spatially …