Services
Two arms of work
The tables below show the source service list at the level of input and output. Each row states its scope limit: what an output is not is as much part of the quote as what it is.
A · Protein design and evaluation
| Service | Input | Output | Scope limit |
|---|---|---|---|
| De novo binder design | Target structure (PDB) or UniProt ID | Ranked candidate sequence library and predicted complexes | The models are predictions; they contain no binding measurement. |
| Epitope-directed design | Target plus the epitope (the surface patch you want engaged) or hotspot | Candidates that engage the specified surface, residue-level contact map | A predicted interaction is not a measured interaction. |
| Protein–protein interface analysis | Complex structure | Binding energy estimate, buried surface area, packing quality, contact list | Energy estimates are not affinity measurements. |
| Paralog selectivity assessment | Target and list of paralogs (related proteins that resemble it) | Epitope conservation rate, residue-level difference table | A sequence and structure assessment, not measured selectivity. |
| Molecular dynamics stability analysis | Complex structure | RMSD/RMSF, contact persistence and a stability summary over the simulated window | Behaviour within the simulated window, not a measured in-cell lifetime. (Claim C10) |
| Mutational effect prediction (ΔΔG) | Structure and mutation list | Per-position stability and binding effect | A prediction, not a measurement. |
| Solubility and aggregation propensity | Sequence or structure | Risk region map, formulation notes | A risk estimate, not an experimental formulation result. |
| Antibody/nanobody modelling and epitope mapping | Sequence or structure | Model, predicted epitope, interface analysis | The model and predicted-epitope labels are kept explicit. |
| Experimental design consultation | Candidate list | Which candidates to test, in what order and format | Running the experiment is not included; this is consultation. |
Detailed page: protein design →
B · Structure-based small-molecule work
| Service | Input | Output | Scope limit |
|---|---|---|---|
| Molecular docking | Target structure and compound list | Ranked poses, score table, interaction fingerprints | A docking score is not a binding free energy. |
| Binding-site and druggability analysis | Target structure | Pocket definition, volume, druggability assessment, hotspot map | — |
| Virtual screening for hit discovery | Target structure and library preference | Filtered and ranked hit list, diversity clustering | A filtering and ranking output; no physical hit is guaranteed. |
| Structure-based optimisation support | Target and starting compound | Analog suggestions with interaction-based rationale | — |
External laboratory
Items coordinated with an external laboratory
This work is run as a service purchase; the provider and scope are stated in writing before the quote. We do not describe the laboratory as if we ran it ourselves.
| Service | Input | Output | Scope limit |
|---|---|---|---|
| Experimental binding measurement (BLI/SPR) | Selected candidate list | Measured binding data or a binding classification | Coordinated as a service purchase from a named external laboratory; the provider is stated in the quote. |
| Recombinant protein production | Candidate sequences | Expressed protein and yield information | An external laboratory item; scope and cost appear as a separate quote line. |
| ADMET profiling | Compound list | Profiling report | An external laboratory item. |
| Solid form prediction | Compound structure | Solid form assessment | Run with an external provider. |
Terms used on this page
New to the field? Start here. The explanations are deliberately short.
- target
- The protein you are working on — the molecule you want to engage, block or detect.
- binder
- A protein designed to stick to the target. Think of it as the key in a lock-and-key pair.
- epitope
- The specific patch on the target’s surface where you want the binding to happen.
- interface
- The surface where two proteins touch. Whether a design works shows up largely here.
- residue
- A single amino acid in the protein chain — one link in the chain.
- paralog
- A related protein that resembles the target. You usually want the design not to bind these by mistake.
- selectivity
- How well a design binds the target while leaving similar proteins alone.
- affinity
- How tightly two molecules hold on to each other. It is measured in the lab, not computed.
- computational
- Work done on a computer. It is not an experiment; it shows which candidate is worth testing.
- complex
- The structure formed by two or more molecules bound together.
- docking
- Computing how a small molecule might sit in a pocket on the target.
- druggability
- How suitable a pocket is for being targeted by a drug-like molecule.
- virtual screening
- Filtering a large set of compounds on a computer to surface the most promising ones.
- molecular dynamics
- Simulating how a structure moves over time — it shows whether a complex holds together.
- ΔΔG
- An estimate of whether a single mutation makes a protein more stable or less.
- aggregation
- Protein molecules clumping together — a common problem in production.
- nanobody
- A single-chain binding protein, much smaller than a conventional antibody.
- BLI / SPR
- Two laboratory methods that actually measure binding — where a computational prediction gets checked.
- RMSD / RMSF
- Measures of how far a structure drifts (RMSD) and which parts wobble most (RMSF) during a simulation.
- UniProt
- The public database of protein sequences and their basic annotations.
- PDB
- The public database of experimentally solved protein structures.
- de novo
- From scratch — designing without an existing candidate or template to start from.
Describe your target briefly and we will settle the scope together.
The first message never asks for confidential sequences, unpublished structures or sensitive files. Technical detail follows an appropriate confidentiality process.