Welcome to the solid-state NMR and dynamics team.
Solid-state NMR and dynamics team. Team leader Paul Schanda.
Our research focus: Understanding the motion of proteins at atomic resolution and the link to molecular function
Understanding protein function at atomic level requires the characterization of protein structure, dynamics and interaction at atomic resolution. While the knowledge of the three-dimensional structures of biomolecules is an important step towards this understanding, many interesting biomolecular processes require that biomolecules dynamically explore a range of different conformational states.
Our main research interest is the characterization of proteins that rely on motion to perform their function. In particular, we are interested in understanding the mechanisms by which membrane proteins transport metabolites through the phospholipid bilayer, and furthermore the modes of action of chaperones interacting with aggregation-prone molecules. We use Nuclear Magnetic Resonance spectroscopy, both in the solid-state and in solution-state to probe structure interactions and dynamics in these systems. In parallel and complementary to these studies of biomolecular function, we actively develop and improve NMR techniques, in particular solid-state NMR approaches, which provide insight into biomolecular dynamics at increasing level of detail.
Native nanodiscs as a tool for membrane protein studies
Sensitive solid-state NMR of large proteins through methyl labeling
Direct observation of the overall rocking motion of a protein in a crystal
A combination of advanced solid-state NMR methods, X-ray crystallography and microsecond-long MD simulations has allowed to demonstrate for the first time the motion of a protein molecule inside a crystal. This motion, occurring on a microsecond time scale, is an important determinant for resolution in X-ray diffraction and solid-state NMR experiments.
Key words: Protein dynamics and mechanisms * Macromolecular machines * Methods development