Determining Protein Structure and Dynamics

Many traditional methods for studying protein structures and dynamics, like X-ray crystallography or cryo-EM, require extreme conditions such as freezing or crystallisation, which can disrupt the protein’s natural behaviour. This makes it hard to understand how proteins function in the real, warm, watery environments of living organisms.

Quantum sensing methods, such as diamond-based magnetometry using nitrogen-vacancy (NV) centres, allows to perform ultra-sensitive magnetic and electric measurements on proteins even in solution and under near-physiological conditions (close to body-like temperatures and environments). These techniques enable the detection of both static structural details and dynamic molecular movements on the nanoscale, without needing invasive or disruptive preparations.

This can provide deeper, more accurate insights into how proteins work in their natural state, improving our understanding of disease mechanisms, advancing drug design, and helping identify new therapeutic targets.