HACKER Q&A
📣 samsamlh

Breakthrough in Protein Folding


Hello HN,

I am reaching out to introduce a major breakthrough in protein folding, allowing complex structures to be accurately modeled in real-time—a significant improvement over traditional Molecular Dynamics (MD) simulations.

Key Achievements

Successful folding of an intrinsically disordered protein (IDP), a challenge for AI-based methods and MD, completed in seconds instead of weeks. Simulation of viral capsid formation, reducing the typical computation time from years to seconds—critical for vaccine and antiviral development. Accurate modeling of membrane proteins, handling steric constraints efficiently while reducing atomic clashes by 98%, surpassing traditional refinement methods. Validated on large multi-domain proteins, achieving correct biologically relevant conformations with exceptionally low computation time.

Why This Matters

Massive Speed Improvement – What previously took weeks or months can now be computed in near real-time. Universal Application – Works for de novo proteins, large assemblies, and constrained environments without requiring extensive computational resources. Potential Drug Discovery Impact – Enables rapid structure-based screening, antibody modeling, and enzyme engineering, accelerating early-stage research.

Next Steps

I can perform the folding of a protein of your choice to show how serious i am, Contact: sam.khedjam@gmail.com

Looking forward to your thoughts,

  👤 Rochus Accepted Answer ✓
Sounds interesting. Since there is already Alphafold, I would assume that your solution concentrates on Alphafold's main weakness: the restriction on cristal structures and steady state, i.e. a single structure snapshot in an unrealistic environment. I would assume that an MD based solution like yours would be able to simulate the movement of structure parts and its interaction with a specific environment. The major challenge of MD so far (as far as I remember) was the computability of decently large proteins in reasonable time. Can you please explain how your solution improves on this? Do you have publications?