Enzyme Engineering
Skip the combinatorial library. Score all single substitutions and select the five most likely to improve catalytic stability.
Learn moreProtSynq scores every point mutation for ΔΔG stability and ΔΔG binding — so enzyme and antibody engineers start wet lab with five ranked variants, not five hundred.
PDB file or AlphaFold model. ProtSynq parses chain topology and identifies all mutable positions.
Maximize thermostability, tune binding affinity for a target chain, or optimize both under a Pareto constraint.
ProtSynq evaluates every single-residue substitution using an ensemble of physics-informed and learned scoring functions.
Five variants ranked by predicted stability and affinity, with per-residue confidence scores and downloadable PDB diffs.
ProtSynq delivers a ranked variant table with per-mutation thermodynamic scores and one-click PDB exports.
| Rank | Variant ID | Mutation | ΔΔG Stability (kcal/mol) | ΔΔG Binding (kcal/mol) | Confidence | Export |
|---|---|---|---|---|---|---|
| #1 | PSQ-LZ-0042 | A123V | −1.84 | −0.62 | 0.91 | |
| #2 | PSQ-LZ-0017 | L87I | −1.51 | −0.38 | 0.88 | |
| #3 | PSQ-LZ-0091 | T204A | −1.29 | +0.11 | 0.83 | |
| #4 | PSQ-LZ-0055 | V316L | −0.97 | −0.44 | 0.76 | |
| #5 | PSQ-LZ-0138 | I251V | −0.82 | +0.07 | 0.72 |
Skip the combinatorial library. Score all single substitutions and select the five most likely to improve catalytic stability.
Learn moreIdentify CDR mutations that improve affinity without destabilizing the VH/VL fold. Filter by predicted Tm shift.
Learn moreEngineer thermostable biocatalysts for high-temperature process conditions — guided by predicted Tm uplift, not trial and error.
Learn moreRequest access to ProtSynq for your next enzyme or antibody campaign.