Protein Dynamics in the Solid State
NMR offers a unique opportunity to study conformational motions and chemical changes on timescales from minutes to picoseconds. Solid state NMR can provide detailed descriptions of motions not possible by other biomolecular techniques, and can also be used to study a wide range of biological systems not appropriate for most other methods. In our lab, we develop methods to disentangle complex motions and achieve clarification of the role of motions in biological function.
Ion Channel Function
Conformational dynamics and transmembrane allosteric coupling in potassium ion channels control channel function — especially timing and excitability. Solid-state NMR investigates conformational equilibria at atomic resolution in ion channels stabilized in near-native liposomes, and provides insights into the effects of ligands.
Protein Oligomerization
Proteins form high-order oligomeric structures with emergent functional phenomena. Solid-state NMR spectroscopy provides a powerful avenue for investigation of the structures, dynamics, functions and mechanisms of these large complexes.