We study how biomolecular function is rooted in dynamics.
Deciphering Biological Mechanisms
How do proteins perform complex tasks such as transporting other proteins across cells, membranes, or into specific compartments like mitochondria? These processes are essential for cellular function and life itself. We study:
- Protein transport mechanisms and chaperoning: Focusing on mitochondrial protein import, we investigate how chaperones, receptors, and translocases are able to transport, translocate and fold large, aggregation-prone polypeptides to their destinations.
- Enzyme dynamics, allostery and evolution: Enzymes are far from being simply rigid catalysts. They display a stunning flexibility, which is often key to substrate entry and turnover, and tuning of their activity. We probe exactly this flexibility to decipher how they work.
Through these studies, we aim to illuminate the intricate mechanisms that underpin cellular organization and function.
Fundamentals of Protein Dynamics
Proteins are not static entities; their motions dictate their actions. We are not only interested in biological mechanisms, but also some fundamental physico-chemical properties of dynamics, such as:
- Active site dynamics: Investigating how subtle motions around an enzyme’s active site influence its catalytic efficiency.
- Molecular flexibility: Examining the movement of side chains, main chains, and entire protein domains in diverse environments, from solutions to crystals to large assemblies.
- Structural packing effects: Understanding how biological assemblies or crystalline environments impact protein dynamics.
- Protein dynamics at extreme conditions: how do proteins behave at very low temperatures? And what is the effect of very high pressure (thousands of bar)?
These studies provide a deeper understanding of the physical principles that govern biomolecular behavior.
Innovating NMR Spectroscopy
Our passion for discovery is matched by our drive to push the boundaries of technology. NMR spectroscopy is at the heart of our research, and we:
- Develop novel methodologies: Creating advanced NMR techniques to make transient “invisible” states of proteins visible, by allying new NMR pulse sequences, tailored isotope labelling and computational methods.
- Probe molecular motions: Designing experiments to precisely map protein dynamics and link them to biological function.
- Integrate complementary methods: Combining NMR with cryo-EM, biophysical, biochemical, computational, and in vivo approaches to provide a comprehensive understanding of biomolecular systems.
Get access to the methods we develop here.
Find out more about our ongoing projects.