Macromolecular crowding affects the activity of proteins and functional macromolecular
complexes in all cells, including bacteria. Crowding, together with physicochemical …

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 …

RNA-dependent DEAD-box ATPases (DDXs) are emerging as major regulators of RNA-
containing membrane-less organelles (MLOs). On the one hand, oligomerizing DDXs can …

Protein-protein and protein-RNA interactions are essential for cell function and survival.
These interactions facilitate the formation of ribonucleoprotein complexes and biomolecular …

Protein misfolding and aggregation are the leading cause of many diseases, including
neuron degenerative diseases, cardiovascular diseases, and cancers. However, the …

The intracellular milieu is crowded with biomacromolecules. Macromolecular crowding
changes the interactions, diffusion, and conformations of biomacromolecules. Changes in …

Aberrant accumulation of protein misfolding can cause aggregation and fibrillation and is
one of the primary characteristic features of neurodegenerative diseases. Because they are …

Many proteins self-associate to achieve function. Macromolecular crowding enhances
protein self-assembly in buffer experiments with added crowders, and crowding could …

Drugging intrinsically disordered proteins (IDPs) has historically been a major challenge
due to their lack of stable binding sites, conformational heterogeneity, and rapid ability to self …

Life as we know it would not exist if proteins did not fold into functional three-dimensional
structures, where α-helices, loops, and β-sheets act together to form active sites that drive a …