Quantum-enabled EPR spectroscopy
Access the inaccessible
Static structures miss the motion that dictates biological function. FATHOM® resolves dynamic behavior.
Structure isn't static.
Cryo-EM, NMR spectroscopy, AlphaFold, and X-ray crystallography give you a snapshot. Biological function lives in what the snapshot misses — the loops that flex, the domains that switch, and the conformational ensembles that drive molecular binding and allosteric regulation.
Measure the motion.
FATHOM resolves nanoscale distance distributions and conformational dynamics on micromolar samples, in under a few hours, on an instrument built for the structural biology lab.
The world's first quantum-enabled EPR spectrometer.
FATHOM measures the protein dynamics that static structural techniques can't resolve — the conformational motion behind binding, signalling, and drug action.
Revolutionizing EPR with Quantum Sensing Technology
Next-generation quantum sensing enhances EPR with greater sensitivity, faster acquisition, and simplified operation. Automated workflows and an intuitive interface enable high-throughput analysis, reducing experiment times from weeks to days.
Superconducting Quantum Sensing
New superconducting quantum-sensing resonator design enables accessible scientific discoveries and higher throughput than classical EPR.
Easy Automated Operation
Load-and-go automated reporting, multi-sample handling and an intuitive touchscreen interface designed for technician-level users.
Short Acquisition Times
Increase in sensitivity, speed and stability reduces EPR acquisition time from weeks to days.
Born from quantum research. Built to transform drug discovery.
High-Q Technologies emerged from the Institute for Quantum Computing at the University of Waterloo. Backed by Quantum Valley Investments and guided by scientific advisors from MIT, we are building the measurement infrastructure for the next generation of structural biology.
Successful site-directed spin labelling (SDSL) starts with proper protein sample preparation. Before the spin-label reagent MTSL can attach to an engineered cysteine, the residue must be available in its reduced thiol form. What happens if cysteine oxidation interferes with labelling, and how can reducing agents such as DTT or TCEP help? Getting this step right is essential for efficient spin-label attachment and reliable EPR measurements.
Site-directed spin labelling (SDSL) is a technique that combines protein engineering with electron paramagnetic resonance (EPR) spectroscopy to investigate protein structure, conformational changes and dynamics.
PROTACs (proteolysis-targeting chimeras) are molecules designed to bring target proteins and E3 ubiquitin ligases together, triggering targeted protein degradation. This makes ternary-complex formation central to PROTAC activity. But their relative positioning and structural arrangement can influence whether degradation occurs. Could DEER spectroscopy reveal how target proteins and E3 ligases are positioned within PROTAC-induced ternary complexes?
