Physics-informed de novo protein design pipeline combining:
- Three-helix bundle scaffold generation optimized for compact binding interfaces
- Iterative charged residue placement (40-46% DEKR) for electrostatic complementarity with NiV-G
- Cysteine minimization for expression robustness in bacterial systems
- Proprietary Target Balance scoring for rapid candidate ranking at proteome scale
- Length optimization (72 AA) based on empirical performance from prior submissions
The pipeline leverages our O(n) linear complexity screening engine to evaluate thousands of variants, selecting designs with optimal interface charge distribution and predicted binding affinity.