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.

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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.