Our research is aimed at understanding mechanism and function in large protein and protein-nucleic acid complexes and assemblies of fundamental importance in biology via atomistic level characterization of biomacromolecular structure, conformational dynamics and interactions. We employ a highly interdisciplinary approach, which includes the development and applications of multidimensional nuclear magnetic resonance (NMR) techniques in the solid-state and in solution, high-resolution cryo-electron microscopy, atomic force microscopy, scanning tunneling electron microscopy as well as complementary biophysical, chemical, molecular biology and computational tools.
The major current research directions include:
- elucidation of the structural basis of strain and cross-seeding barrier phenomena in mammalian prion protein amyloids
- characterization of chromatin structure, dynamics and interactions with particular focus on the role of dynamic histone protein tail domains in mediating chromatin compaction and interactions with regulatory proteins
- characterization of DNA base pairing and hydrogen bonding in large protein-DNA complexes
- development of paramagnetic solid-state NMR methods for rapid protein structure determination
For the most detailed and up-to-date information on our research please see the publications page.