Uncoupling of dynamin polymerization and GTPase activity can be induced with dynamin, which allows in vivo visualization of its activity at endocytic pits.
Single molecule subunit counting, FRET and electrophysiology experiments reveal that metabotropic glutamate receptor subunits interact and rearrange at the level of the transmembrane domains in response to allosteric modulators.
High-speed atomic force microscopy reveals that the open state of the divalent ion channel CorA is highly dynamic and defined by the fast exchange between conformations.
Selective import via bacterial ABC importers is facilitated by a hitherto unrecognized complexity in the conformational dynamics of the substrate-binding proteins.
A combination of X-ray crystallography, molecular dynamics and small angle X-ray scattering shows that the transcription antiterminator M2-1 is a structurally dynamic homotetramer that undergoes large concerted conformational changes upon binding its target RNA.
Single-molecule measurement of conformational dynamics using a genetically encoded fluorescent probe suggests that the selectivity filter region of TRPV1 channels undergoes dynamic motion during agonist activation.
Integrated experimental-computational approaches were implemented to reveal the dynamic conformational landscape of a biologically relevant protein methyltransferase SETD8 for functional annotation.
The conformational dynamics of multidrug resistance protein 1 (MRP1) are tracked in real time by single-molecule fluorescence resonance energy transfer experiments, which elucidate the rate-limiting mechanism of MRP1's transport cycle.
