Binding of a charged small molecule to a membrane protein changes the amplitude of the apparent membrane capacitance by changing the charge density at the surfaces of the membrane.

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.

ER-resident chaperones and cargo receptors make excursions to the cell surface and endocytic compartments when they accompany misfolded clients to lysosomes for degradation.

ESCRT-III heteropolymers utilize non-specific lateral electrostatic interactions to recognize one another, which may enable the polymers to slide along one another and adapt to different curvatures.

Phosphatidic acid influences the gating of voltage-gated K+ channels through a non-specific surface charge mechanism and through a specific interaction between a voltage sensor arginine and the primary phosphate head group on the cytoplasmic membrane leaflet.

Some species of bats hunt for insects that are resting on surfaces by detecting interruptions in the echoes from that surface, suggesting that resting on rough surfaces may help insects to evade detection by echolocation.

Oligomerization of p62/SQSTM1 generates high avidity binding regions that enable it to spatially select for concentrated ubiquitin and ATG8-family proteins.

Cellular hallmarks of thermal limits are evolutionarily conserved in nematodes, and changes in surface to volume ratio reflect restricted aerobic metabolism at these limits.

The number of contacts at the interface of a protein–protein complex, together with the properties of the surface, provides a simple, but well-performing predictor of binding affinity.

Mutations that block assembly of the interlocked RcsF/β barrel protein complex prevent detection of lipopolysaccharide stress and activation of Rcs signal transduction pathway.