ABOUT HIGH Q TECHNOLOGIES
High Q Technologies, based in Waterloo, Ontario, develops quantum‑sensing EPR systems that empower structural biologists, pharmaceutical researchers, and biotechnology teams with high‑resolution, ground‑truth insights into protein behavior. Our flagship instrument, FATHOM®, is the world’s first quantum‑sensing EPR spectrometer, purpose‑built to reveal protein conformations, distance distributions, and dynamics with a level of industry accessible precision unattainable through conventional techniques.
FATHOM’s innovative resonator design and automated workflows streamline operation across multiple samples, dramatically reducing acquisition times while capturing protein motions that are often invisible to traditional structural methods. These capabilities make FATHOM a powerful complement to Cryo‑EM, AlphaFold predictions, and molecular dynamics simulations, providing experimental validation that strengthens mechanistic understanding.
For pharmaceutical drug discovery teams, FATHOM provides differentiated, quantum‑enabled experimental validation that sharpens decision‑making. By confirming mechanism engagement, exposing state‑specific liabilities often missed by conventional assays, and improving compound prioritization, FATHOM reduces the risk of advancing molecules with hidden mechanistic flaws. This iterative feedback improves decision quality across hit validation and lead optimization, enabling drug discovery teams to progress candidates with greater confidence.
At the intersection of AI drug design, experimental structural biology, and proprietary training data, High Q Technologies and the FATHOM platform deliver quantum‑enabled ground‑truth capability. The next bottleneck in AI‑driven drug discovery is determining which AI‑designed molecules actually produce the intended biological mechanism. FATHOM provides an iterative experimental feedback layer that enhances mechanism confidence, improves compound ranking, and reveals state‑specific risk flags across in-silico hit validation and lead optimization. This strengthens candidate selection before substantial downstream development resources are committed, helping partners mitigate a significant driver of late‑stage clinical failure.
To support researchers who do not yet have in‑house EPR capabilities, High Q Technologies also offers a Sample Measurement Service (SMS). This flexible, low friction service readily provides access to FATHOM analysis’, from a single‑sample project to fully managed measurement pipelines, allowing teams to integrate FATHOM’s experimental insights directly into their discovery workflows.
For more information, visit www.highqtechnologies.com.
FEATURED ARTICLES
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How EPR Unlocks Missing Dynamics In Pharma And Structural Biology Workflow
Uncover how EPR spectroscopy fills the conformational gap by capturing dynamic protein motions, refining Cryo-EM models, and revealing hidden structural ensembles for drug discovery.
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Spin Class: DEER In The Spotlight
Explore how EPR-based distance measurement techniques differ in implementation, optimization, and strengths, as well as which sample characteristics can help determine the most suitable approach.
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Applications Of EPR Spectroscopy In Structural Biology Workflows
Gain insight into how EPR spectroscopy reveals protein dynamics, validates structural models, supports Cryo-EM sample screening, and characterizes GPCR conformational changes.
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Why Protein Motion Matters As Much As Protein Structure
Protein structures are not static. See how conformational changes influence physiological function and how electron paramagnetic resonance spectroscopy provides insights into effective design.
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5 Ways FATHOM EPR Complements NMR
See how EPR extends structural analysis beyond conventional NMR constraints by revealing long-range distances, conformational heterogeneity, paramagnetic centers, and more.
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How Does EPR Spectroscopy Complement Cryo-EM?
Discover how EPR complements structural maps by resolving flexible regions, detecting hidden conformational states, identifying differences between grid-based and solution conditions, and revealing the dynamic changes that connect molecular structure with biological function.
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7 Causes Of Unresolved Density And How To Investigate Them
Missing cryo-EM density does not always indicate disorder. Learn how flexibility, conformational variation, incomplete occupancy, and sample heterogeneity can shape what is visible in a protein structure.
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NMR And EPR Spectroscopy: A Complementary Approach For Protein Dynamics
Discover how pulsed dipolar EPR complements NMR by revealing protein flexibility, conformational changes, and ligand-induced dynamics, including low-population states that can be difficult to resolve.
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EPR Pulsed Dipolar Spectroscopy For Structural Biology
Discover how automated EPR pulsed dipolar spectroscopy measures protein dynamics, complements Cryo-EM and AlphaFold, and delivers crucial structural insights for drug discovery.
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How EPR Spectroscopy Reveals Membrane Protein Structure And Dynamics
Resolving dynamic states in membrane proteins is vital for drug discovery. EPR spectroscopy tracks conformational shifts in native environments, bypassing standard structural limits.
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What Is EPR Spectroscopy? Principles, Spin Labeling, And DEER In Proteins
Capturing dynamic biomolecular motion remains crucial for research. EPR spectroscopy delivers ensemble distance distributions to resolve flexible states in complex protein systems.
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Spin Class: Putting A Label On It
Uncover how selecting the right site-directed spin label enhances EPR spectroscopy, enabling precise biomolecular structural insights and robust in-cell measurements.
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How EPR Unlocks Missing Dynamics In Integrative Structural Biology
Explore how pulse dipolar spectroscopy captures dynamic conformational ensembles, refining structural models alongside cryo-EM and AI tools to accelerate drug discovery.
CONTACT INFORMATION
High Q Technologies
485 Wes Graham Way
Waterloo, ON N2L 0A7
CANADA
Contact: Glen Gregory
SOLUTIONS
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Protein dynamics can expose critical gaps between computational predictions and biological behavior. Learn how experimentally measuring conformational states can strengthen model validation.
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Capturing dynamic conformational states is key to target druggability. Advanced EPR spectroscopy delivers nanometer-resolution measurements for complex structural biology.
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Quantum-enabled spectroscopy delivers high sensitivity with minimal sample volumes, complementing cryo-EM and NMR to resolve complex protein structures.
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Observe automated cryogenic sample loading and measurement execution designed to standardize sample handling and improve precision in spectroscopic analysis.
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Streamline structural biology research by outsourcing specialized sample measurements to receive comprehensive distance distributions and publication-ready analytical reports.