Solid state NMR is unable to detect any association of substrate to the second binding site, S2, in the extracellular vestibule of the Neurotransmitter:Sodium Symporter LeuT.

NDR kinase Orb6 prevents RNP granule assembly and translational repression by promoting Sts5 association with 14-3-3 protein Rad24 to spatially control polarized cell growth.

Nuclear magnetic resonance analysis revealed the structural and dynamical changes in MgtE during the channel closure caused by the cooperative Mg²⁺-binding, which had remained undescribed only by a static crystal structure.

NMR studies settle part of a long-standing debate about the mechanism used by the Hsp70 chaperone to recognize substrates.

Translation pauses occur in strategic positions to facilitate the production of properly folded membrane proteins in bacteria.

Light signaling components interact with a histone H2B deubiquitination module, adjusting chromatin states at global level during Arabidopsis seedling development.

A combined NMR and kinetic study demonstrates how the dynamic transition of a molecular chaperone between different oligomerization states can modulate its activity by altering the binding kinetics and energetics of non-native proteins.

NMR-based flux measurements show that both bacterial and human Hsp70 chaperones interact with helical, as well as sheet substrates predominantly through a conformational selection mechanism.