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.

A simple label-free method uses the electrical properties of cells to detect how ligands bind to membrane proteins.

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.

Distinct binding of viral proteins to the same region on the nucleosome surface can result in contrasting changes to higher-order chromatin structure in the host cell.

Imaging, quantitative immunoblotting and mass spectrometry reveal that hundreds of surface-expressed neuronal membrane proteins exhibit atypical glycosylation profiles, resulting in changes in protein half-life and synaptic responses.

MorphoGraphX summarizes full 3D datasets as curved surface images (2.5D), enabling the efficient quantification of growth and gene expression data from large time-lapse volumetric datasets.

Hydrogen-Deuterium exchange experiments show that Ric-8A induces similar dynamic changes in the structure of Gα as G protein-coupled receptors, yet protects a larger surface of the nucleotide-binding Ras domain.

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.

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