At AI|ffinity, we are pioneers in leveraging the synergy of Nuclear Magnetic Resonance (NMR) 🧲 and Artificial Intelligence (AI) 🧠 to forge unprecedented pathways in drug development. We offer protein(-ligand) structure determination services by our proprietary 4D NMR technology. Our ML-based software, 4D-GRAPHS, enables automatic, all protein atom resonance assignment and structure determination from no more than two NMR spectra, thus reducing remarkably the time and costs.

✅ Advantages:

• Suitable for flexible proteins: if they are soluble and stable at concentrations as low as 0.1-0.2 mM, with the typical range being 0.2 mM to 1 mM; non need for crystallization.

• Speed and Cost-Effectiveness: up to 6x faster and 3x cheaper than X-ray crystallography and up to 2x faster than standard 3D NMR methods.

• Handling Larger Proteins: thanks to the enhanced 4D peak resolution.

• Less Human Input: streamlined spectrum analysis and structure calculations reduce human intervention and related errors.

• Market-Leading Speed: only one 4D spectrum is needed for follow-up structures, such as mutants or protein-ligand complexes.

• Insight Into Protein Dynamics: and mechanisms of action.

• Mapping Interactions: with other molecules and is ideal for weak binders (hit compounds), offering a competitive edge.

• Natural Environment Representation: unlike X-ray crystallography and Cryo-EM that provide structural information about proteins in an artificially "frozen" state.

• No Installation Needed: the algorithm and all necessary software for structure calculations will be provided as a cloud service, including technical support.

❌ Current Method Limitations:

• Protein Size Limit: at ~30 kDa, although this limit is expected to increase with new Ultra-high field NMR spectrometers (1.2 GHz).

• Dependence on Third-Party Software: for raw spectra processing, which can make the pipeline more complex, though this issue is common to all NMR software for resonance assignment.

• Requirement for High Protein Concentrations: typically 0.5 mM to 2 mM for globular proteins, with larger ones often requiring the upper end for adequate signal-to-noise ratios, risking potential aggregation or precipitation.

📩 If you would like to collaborate with AI|ffinity, please provide us with a non-confidential proposal along with scientific supporting data / needs  in your application.