We use Nuclear Magnetic Resonance (NMR) methods to investigate complex biological mechanisms, including protein folding and misfolding, and chaperone mediated proteostasis. By combining NMR with fluorescence-based techniques, mass spectrometry and electron microscopy we aim to develop new approaches that visualize these events across the microscopic to the macroscopic scales.
The group has local access to state of the art NMR spectrometers (solution 400, 600, 800 MHz, solid-state 600 MHz) and many other world-class facilities (950 MHz, electron microscopy) hosted in the nearby Francis-Crick Institute.
Studying lowly-populated, biologically important, protein states that are not accessible by other methods is a keen interest for the lab.
The Hsp40-Hsp70 cycle
Of particular interest is the study of the mechanisms that Hsp40s use to cooperate with Hsp70, a crucial component for cell integrity
We aim to develop integrative/computational approaches that combine experimental data with AI models to study complex systems