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.
The THAP-domain protein Bip1, along with other proteins Nup98 and RpS8, controls the expression of the protein Pvr, a critical non-cell-autonomous regulator of Drosophila blood progenitor maintenance.
A heterodimeric exporter exhibits conformational equilibria in the presence of nucleotides, suggesting a unified mechanistic model for the conformational cycle of ABC exporters.
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.
The molecular chaperone BIP from the endoplasmic reticulum is fine-tuned postranslationally through the thermodynamic and kinetic alterations in its conformational ensemble of functionally and structurally distinct physiological forms.
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.
Point mutations in a ubiquitous human ATPase called p97/VCP deregulate inter-domain communication, resulting in impaired binding of an adaptor that recruits p97 to endosomal pathways and leading to a degenerative disease of bone, muscle and neurons.
