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 …

Biochemical processes take place in heterogeneous and highly volume-occupied or
crowded environments that can considerably influence the reactivity and distribution of …

A variety of excipients are used to stabilize proteins, suppress protein aggregation, reduce
surface adsorption, or to simply provide physiological osmolality. The stabilizers encompass …

In recent years, better instrumentation and greater computing power have enabled the
imaging of elusive biomolecule dynamics in cells, driving many advances in understanding …

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

In recent years significant effort has been devoted to exploring the potential effects of
macromolecular crowding on protein folding and association phenomena. Theoretical …

Abstract Effects of macromolecular crowding on structural and functional properties of
ordered proteins, their folding, interactability, and aggregation are well documented. Much …

Recent experiments inside cells and in cytomimetic conditions have demonstrated that the
crowded environments found therein can significantly reshape the energy landscapes of …

Background The environment inside cells in which proteins fold and function are quite
different from that of the dilute buffer solutions often used during in vitro experiments. The …