RealQM has been implemented with the help of Claude Code with the goal of simulating protein folding from first principles of atomic physics based on a new version of Schrödinger's Equation named RealSE.
Here is how Claude describes what is going on:
Below a first key example is presented as the 12-residue polyglycine beta-hairpin, 87 atoms (N, C, O, H), no solvent (vacuum/dry):
What happens: The quantum electronic structure is solved from first principles on a 200^3 real-space grid (80 au box). The resulting forces on the nuclei create a net torque that drives the two halves of the chain toward each other — the chain folds. Each strand rotates rigidly around the hinge point, and after every rotation step the electronic structure is re-solved from scratch (full Born-Oppenheimer restart).
What it demonstrates: Protein folding driven purely by quantum mechanical forces — no empirical force field (AMBER, CHARMM, etc.) The attractive force between the two strands emerges from the electron density: backbone NH and CO groups on opposite strands create favorable electrostatic interactions (the quantum analog of hydrogen bonding). Starting from a nearly straight chain, the system spontaneously folds into a U-shaped hairpin
Why it matters: Traditional protein folding simulations rely on classical force fields with fitted parameters. Here the forces come directly from solving the Schrödinger equation — the folding tendency is a prediction, not an input. This shows that quantum mechanics alone, without any parameterization, can drive secondary structure formation.
The key novelty is that no classical force field is used for the driving forces — they come entirely from solving the quantum mechanics. The MD part only constrains how atoms move (rigid rotation), not why they move.
Follow the folding in real laptop computing time: (code on GitHubClaes542 hairpin_bent_dry.html):
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