High Q Technologies and Creative Biostructure have formed a strategic partnership to expand access to a new approach for studying protein behavior, particularly for applications in pharmaceutical and biotechnology research. Recognizing limitations in traditional methods for analyzing flexible and disordered proteins, increasingly relevant targets in drug discovery, the collaboration aims to overcome barriers to electron paramagnetic resonance (EPR) spectroscopy adoption. Leveraging quantum sensor technology, High Q Technologies’ FATHOM EPR platform measures long-range distances, allowing researchers to probe conformational changes and molecular motion linked to conditions driven by protein aggregation and dynamic intermediates. “Drug discovery is increasingly focused on understanding how proteins behave in motion,” said Don Carkner, Managing Director at High Q Technologies. “With FATHOM, quantum-enabled EPR spectroscopy provides a way to study these dynamic systems, and through this partnership with Creative Biostructure, we are making these capabilities more accessible within structural biology and drug discovery workflows.”
FATHOM EPR spectroscopy, developed by High Q Technologies, addresses a critical gap in structural biology by allowing researchers to move beyond static protein models and investigate the dynamics of intrinsically disordered proteins increasingly implicated in disease. Tony Zhang, Principal Scientist at Creative Biostructure, stated that EPR spectroscopy adds dynamic information that complements methods such as cryo-EM, NMR spectroscopy, and computational modeling, highlighting the platform’s potential to integrate with existing structural biology techniques.
Creative Biostructure, a structural biology Contract Research Organization, is collaborating with High Q Technologies to broaden access to advanced protein dynamics research utilizing quantum-enabled electron paramagnetic resonance (EPR) spectroscopy. This partnership addresses a growing need within pharmaceutical and biotechnology sectors as drug discovery increasingly focuses on disordered, flexible proteins, systems poorly characterized by traditional static structural methods.
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
