On this page
Free to start

Know which mutations will work before you spend weeks in the lab.

Published · Updated

NeuroAutomata scores every possible amino acid substitution at every position in your protein. Paste a sequence, get a fitness landscape in seconds. Download everything. Your sequences are processed in memory and deleted from our systems within an hour.

Sign up

What Is NeuroAutomata

NeuroAutomata is a web-based protein mutation scoring tool built on ESM-2, a protein language model developed by Meta AI and trained on millions of protein sequences from across the tree of life. Think of it as a second opinion on your mutagenesis experiments — one that's read every protein sequence in UniProt.

NeuroAutomata now also supports ESMC, a protein language model family released under an open MIT license (commercial use included) by the Chan Zuckerberg Biohub — the nonprofit research institute the original ESM team joined in late 2025. Because it's openly licensed, we can offer it to you directly.

You can choose the model that fits your work:

ModelSizeModel cardEmbedding dimRuns on
ESM-2 650M (default)650Mfacebook/esm2_t33_650M_UR50D1280T4 GPU
ESMC 600M600Mbiohub/ESMC-600M1152T4 GPU
ESMC 6B (experimental)6Bbiohub/ESMC-6B2560A100 GPU

You paste a sequence, and NeuroAutomata predicts which mutations are likely tolerable and which ones will probably break your protein. It works on any protein from any organism — even sequences that have never been experimentally characterized — because its predictions come from evolutionary patterns across all known protein families, not from labeled training data specific to your protein.

It runs in your browser. There's nothing to install. Every result you generate — charts and raw scores — is downloadable. Your sequences are processed in memory and deleted from our systems within an hour. Full details in our privacy policy.

NeuroAutomata is built for protein engineers, biochemists, and anyone running mutagenesis on their own proteins. It is free to start, with no card required. Run it on your sequences and tell us what works and what we should fix.

It Already Knew About EGFP

In 1995, Roger Tsien's lab mutated Serine 65 to Threonine in jellyfish GFP and created EGFP — the most widely used fluorescent protein in biology. We ran wild-type GFP (P42212) through NeuroAutomata. In under 30 seconds, it scored S65T as tolerable (-0.137) while flagging S65W and S65C as harmful. It identified the exact mutation that changed biology — without any GFP-specific training data.

GFP mutation landscape heatmap — 238 positions scored across all 20 amino acid substitutions. Blue indicates tolerable mutations, red indicates likely destructive mutations.
Every position in GFP, every possible substitution. Blue is tolerable. Red is likely destructive. At a glance: most of GFP is safe to engineer — but those red columns are positions you cannot touch.
GFP per-position sensitivity chart showing mutation tolerance across all 238 residues.
Which residues tolerate change — and which ones don't.
Single mutation analysis of S65T in GFP — scored as tolerable at -0.137, confirming the EGFP mutation.
S65T: the mutation that created EGFP. NeuroAutomata scores it as tolerable.

See It in Action

We loaded 9 proteins — fluorescent reporters, therapeutic targets, industrial enzymes, and a CRISPR domain — and scored all of them. Before running any mutations, NeuroAutomata shows you how your proteins relate to each other.

Protein similarity map showing 9 demo proteins — fluorescent proteins cluster together, enzymes group, therapeutic targets separate.
GFP and mCherry cluster together — both are fluorescent beta-barrels, but from completely different organisms. KRAS sits alone. Ubiquitin is an outlier. These groupings come from the protein sequences themselves, not from any labels we provided.

How It Works

1

Paste your sequence

Amino acid sequence or FASTA format. Up to 1,024 residues. You can also load example proteins to explore first.

2

Generate a protein fingerprint

The AI model reads your sequence and creates a numerical representation that captures what makes your protein unique — its evolutionary history, structural tendencies, and functional constraints.

3

Compare your proteins

Load multiple sequences and see which ones are related and which aren't. Proteins with similar functions cluster together — even across organisms.

4

Score every possible mutation

All 20 amino acid substitutions at every position, scored automatically. The heatmap shows you which mutations are tolerated (blue) and which are likely destructive (red) — so you know where to focus before running a single experiment.

5

See it in 3D

Mutation tolerance scores mapped onto your protein's 3D structure. Blue residues are safe to change. Red residues are conserved. See exactly where your planned mutations sit in physical space.

What It Found in GFP

The underlying model was trained on millions of protein sequences from across the tree of life. It learned which positions matter and which are flexible — without being told anything about structure, function, or experimental data. When we scored GFP:

S65T
-0.137 — tolerable. The model says "this is fine." It was. This mutation created EGFP, the most used fluorescent protein in history — work that contributed to the 2008 Nobel Prize in Chemistry.
S65W
Predicted harmful. A bulky tryptophan at this position would disrupt the chromophore — the part of GFP that actually produces fluorescence.
C48D
+3.39 — predicted most beneficial. Free cysteines cause proteins to aggregate and misfold. Protein engineers have independently targeted this exact position to improve GFP stability.

Nobody told the model about the GFP chromophore. Nobody provided GFP-specific training data. It figured this out from sequence patterns alone, in 30 seconds.

Validated Against Real Experiments

We checked NeuroAutomata's predictions against published experimental data: deep mutational scanning results from ProteinGym, a reference benchmark where researchers made the mutations in the lab and measured what each one did. These are clinically and pharmacologically real proteins, not toy examples. They include cancer-associated tumor suppressors, drug-metabolizing and drug-dosing enzymes, and a cell-surface receptor.

ProteinWhat the experiment measuredRank correlation
Insulin receptor (INSR)Insulin binding0.3989
CYP2C9Enzyme activity0.679
CYP2C9Protein abundance0.634
BRCA1 (RING domain)Gene function0.409
BRCA1 (BRCT domain)Gene function0.534
PTENProtein abundance0.484
TPMTProtein abundance0.5298

Across these seven measurements, the median rank correlation is 0.5298. For scale, ESM-2 650M, NeuroAutomata's default model, averages 0.414 across the full ProteinGym benchmark of 217 assays (leaderboard CSV, accessed 2026-05-08). Most of this cohort lands above that benchmark-wide average, though not all of it does.

Where the model is weakest is binding. The two lowest scores are both binding measurements: the insulin receptor at 0.3989, and calmodulin, a calcium-sensing protein we also benchmarked, at 0.212, which is well below the model's own 217-assay average. We report this alongside the strong results rather than burying it. The in-app Learn section walks through the full method: what it does well, and where it falls short.

What Happens to Your Sequences

Your sequences are processed in memory, held in a temporary queue for up to one hour so you can download your results, and then automatically deleted. Nothing is saved to disk. We don't train models on your data. Everything you generate is downloadable, so keep the results you want.

Some processing runs on external services. Running your sequence through the model (embeddings, mutation scoring, and landscape scans) happens on a contracted GPU provider that acts as our data processor. Structure prediction sends your sequence to a separate third-party public API that we don't control. Our privacy policy names each provider and explains how your data is handled.

What You Get

  • Works in your browser — nothing to install, nothing to configure
  • Results in seconds — not days, not hours
  • Works on any protein — from any organism, even ones never studied before
  • Download everything you generate — charts and raw data as CSV. Your results, your files.

Use It in Claude and ChatGPT

Run NeuroAutomata where you already work. Add it as a custom connector (currently a beta feature in both assistants) with one URL: works on every Claude plan, and on paid ChatGPT plans with Developer mode turned on. Read the guide →

Plans

NeuroAutomata is open to everyone. Start free, no card required. Upgrade when you need the heavier models and full landscape scans. We are still calibrating what sits where, so plans will keep moving as testers tell us what they need.

Free

$0

Everything you need to start scoring mutations.

  • Protein embeddings
  • Single-mutation scoring
  • Protein comparison and visualization
  • Download your results (CSV and chart exports)

Standard throughput

Pro

$9.99/mo
Introductory test pricing

The full mutation-intelligence workbench.

Everything in Free, plus:

  • ESMC-6B embeddings (our largest, experimental model)
  • ESMFold structure prediction (PDB structure fetch stays free)
  • Full mutation landscape scans (downloadable heatmap across every position)
  • Per-residue embeddings

Higher limits and more concurrent jobs

Start free

No card required. The free tier stays free.

Plans are in active testing. Limits and the free/pro line may change as we learn how researchers actually use the tool.