ATP consumption enables chaperones to exploit the different kinetic properties of their conformational states to exhibit a non-equilibrium affinity for their substrates that is orders of magnitude higher than its equilibrium value.
Measuring the equilibrium dimerization of a polytopic membrane protein in lipid bilayers forms the basis of a new system for studying the physical forces that stabilize membrane protein association in membranes.
Liquid-liquid phase separation of tau is demonstrated to be an equilibrium state, stable only within a narrow range near physiological conditions, and thus has the capacity to regulate biological processes.
A combination of equilibrium and nonequilibrium molecular dynamics simulations is an effective tool to study allosteric communications in ultrafast enzymes that show little or no conformational changes.
Single-cell FRET measurements reveal large temporal activity fluctuations within this signaling pathway in Escherichia coli, caused by stochasticity of receptor methylation combined with allosteric interactions and slow rearrangements within receptor clusters.