Macromolecular crowding has long been known to significantly affect protein
oligomerization, and yet no direct quantitative measurements appear to have been made of …

The crowded environments inside cells can have significant effects on the folding stability
and other biophysical properties of proteins. In this study on how macromolecular crowding …

The generic tendency of proteins to aggregate into non-functional, and sometimes cytotoxic,
structures poses a universal problem for all types of cell. This tendency is greatly …

The intracellular environment contains high concentrations of macromolecules occupying up
to 30% of the total cellular volume. Presence of these macromolecules decreases the …

Macromolecular crowding in cells is recognized to have a significant impact on biological
function, yet quantitative models for its effects are relatively undeveloped. The influence of …

Highlights•Crowding is probably less extreme than believed in cytosol but still important in
compartments.•Volume exclusion due to crowding and confinement ought to stabilize …

The intracellular environment represents an extremely crowded milieu, with a limited amount
of free water and an almost complete lack of unoccupied space. Obviously, slightly salted …

Protein− protein interactions are usually studied in dilute buffered solutions with
macromolecule concentrations of< 10 g/L. In cells, however, the macromolecule …

Theoretical models predict that macromolecular crowding can increase protein folding
stability, but depending on details of the models (eg, how the denatured state is …

Background Solutions containing high macromolecule concentrations are predicted to affect
a number of protein properties compared to those properties in dilute solution. In cells, these …