Conservative mutations within a secondary active transport protein influenced the conformational equilibrium probed using NMR spectroscopy which correlated to the functional output in vivo.

The intermediate state conformation of the human KCNQ1 potassium channel voltage sensor domain was determined, validated, and shown to be conductive under physiological conditions.

Interactions with Sm proteins can provide a way in which regulatory factors can modulate alternative splice site choices.

An NMR-based structural study of sperm proteins reveals a novel protein packaging/dispersion system embedded in a coevolutionary arms race.

The BPTF PHD finger is inhibited from binding the methylated H3 tails in the context of the nucleosome due to their robust interaction with the nucleosomal DNA, which can be modulated by additional histone PTMs.

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.

Post-translational modifications regulate transient protein-protein interactions to disrupt Ubiquitin enzyme/ligase complexes, a strategy used by Shigella to inactivate the host immune response.

Product release from human lysozyme is mediated by an intermediate state with transient weak interactions between the product and enzyme.

Solution NMR spectroscopy reveals the energy landscape of immature Cu, Zn-superoxide dismutase and leads to atomic resolution structural models of transiently populated non-native oligomers.

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