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.

External calcium regulates neuronal excitability via its actions on voltage-gated sodium channels but not by regulating NALCN via the calcium-sensing receptor.

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

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.

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.

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.

Ancestral sequence reconstruction of an essential muscle protein involved in oxygen storage and transport accurately tracks secondary aquatic transitions in a speciose clade of insectivorous mammals.

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.