Our research is centered on the development of nuclear magnetic resonance (NMR) techniques with the goal of providing insight into the structure, dynamics and interactions of biological macromolecules at atomic resolution. The primary focus of the group is on magic-angle spinning (MAS) solid-state NMR, but we also employ modern solution-state NMR techniques.
We are particularly interested in the development of multidimensional solid-state NMR pulse sequences, which enable the determination of local and long-range structural restraints, such as dihedral angles and internuclear distances, at multiple sites in the protein and with high precision and accuracy. The newly developed NMR methods are applied to both fundamental studies of protein structure, dynamics and interactions in the solid phase, and the atomic-level characterization of biomacromolecules, which are difficult to investigate using traditional high-resolution techniques. Examples include peptides and proteins, which self-assemble into supramolecular aggregates and are associated with protein misfolding disorders (e.g., Alzheimer's and prion diseases), membrane-associated peptides and proteins, and other large macromolecular complexes.
The research carried out in the group is highly interdisciplinary. In addition to NMR spectroscopy, we use computational and biophysical methods, and chemical and molecular biology approaches to the synthesis and purification of isotope labeled peptides and proteins.
For the most detailed and up-to-date information on our research please see the publications page.