High Q Technologies and Creative Biostructure have formed a strategic partnership to expand access to a new approach in studying protein behavior, leveraging quantum-enabled electron paramagnetic resonance (EPR) spectroscopy. Historically limited by complex instrumentation and specialized expertise, EPR spectroscopy is gaining prominence as drug discovery increasingly focuses on flexible protein systems that static methods cannot fully capture. FATHOM EPR, developed by High Q Technologies, utilizes quantum sensor technology to overcome these hurdles, providing unique measurements of long-range distances to probe conformational changes linked to diseases driven by protein misfolding and dynamic processes. “Drug discovery is increasingly focused on understanding how proteins behave in motion,” said Don Carkner, Managing Director at High Q Technologies. Through this collaboration, the companies aim to integrate these dynamic insights into structural biology and drug discovery workflows.
FATHOM EPR Spectroscopy Measures Protein Dynamics & Conformational Ensembles
The system’s advancement stems from the integration of quantum sensor technology, addressing historical limitations of instrument complexity and the specialized expertise required for both experimental setup and data analysis. This ability to probe dynamic systems is particularly relevant for health conditions driven by intrinsic disorder, where static structural analysis provides an incomplete picture; FATHOM EPR’s measurements offer insight into the functional relevance of these fluctuating protein states. Creative Biostructure’s partnership with High Q Technologies aims to broaden access to this technology, providing scientific consultation and workflow support for organizations adopting the FATHOM platform. Tony Zhang, Principal Scientist at Creative Biostructure, notes that EPR spectroscopy complements existing structural biology techniques like cryo-EM and NMR spectroscopy, adding a crucial layer of dynamic information.
The pursuit of effective therapeutics is increasingly reliant on characterizing protein motion, a shift demanding advanced biophysical techniques beyond traditional static structural analysis. Understanding these motions is crucial for developing drugs that target proteins effectively, and this technology offers a new avenue for investigation.
EPR spectroscopy adds an important layer of dynamic information that complements methods such as cryo-EM, NMR spectroscopy, and computational modeling.
Tony Zhang, Principal Scientist at Creative Biostructure
