Diffusion of differently sized proteins in bacterial cytoplasm is nearly Brownian and consistent with the Stokes-Einstein relation, once protein shape and cell geometry are taken into account, and effects of various perturbation can be described as changes in cytoplasmic viscosity.

The volume of the nucleus is dictated by a balance of colloid osmotic forces from the nucleoplasm and cytoplasm.

The cytoplasm behaves as an adaptable fluid that can reversibly transition into a protective solid-like state upon stress.

Crowding and metabolites in a simulated cellular environment alter protein conformations, modulate interactions of functionally related proteins, and lead to significant dynamic heterogeneity.

Weak yet highly species-specific protein-protein interactions enhance the activity of metabolically related enzymes in bacteria at endogenous conditions, but also mean that overexpression of one partner leads to permanent non-physiological complexes and gene dosage toxicity.

In mitotically aging yeast cells, the cytosol acidifies, the distances between the organellar membranes decrease dramatically, but crowding on the scale of the average size protein is relatively stable.

A cell-sized fully confined space significantly controls the emergence and stability of a protein wave, resulting in intracellular spatiotemporal regulation driven by a reaction-diffusion mechanism.

Bacterial cytoplasmic chemoreceptors assemble into a sandwich of two hexagonally packed arrays.

Transcription factors form clusters independently of the presence of DNA, which regulate target genes as opposed to individual monomers, addressing a longstanding question of how transcription factors can find gene targets so quickly.

The diffusion coefficients of proteins in the cytoplasm depend on their net charge and the distribution of charge over the protein surface, with positive proteins moving up to 100-fold slower because they bind to ribosomes.