Compute Topological Fingerprint (TDA)
compute_topology_fingerprintCompute a rotation-invariant topological fingerprint of a protein's fold using persistent homology, outputting a 64-dimensional vector and Betti numbers for structure-similarity comparisons.
Instructions
Compute a rotation-invariant topological fingerprint of a protein's fold.
Fetches the AlphaFold model for uniprot_id and runs persistent homology
(a Vietoris-Rips filtration over the Cα point cloud) to produce a
64-dimensional fingerprint vector plus Betti numbers β₀, β₁, β₂. Use it as the
per-protein input to structure-similarity comparisons:
compare_proteins_topologically and find_evolutionary_structural_shifts
consume these fingerprints.
The Betti numbers summarise fold topology: β₀ counts connected components (single- vs multi-domain or fragmented chains), β₁ counts loops/holes (β-barrels, large macrocycles), β₂ counts enclosed voids (cavities). Because they are invariant to rotation and translation, two orientations of the same fold produce the same fingerprint.
Returns the fingerprint vector, the Betti numbers, the residue count, and which
method ran. Full persistent homology needs the optional [tda] extra
(gudhi); without it a coarse fallback runs that does NOT compute persistent
homology, and the result flags this. Returns a no-structure result when
AlphaFold DB has no model for the accession. This is a coarse, geometry-only
summary — not a substitute for sequence alignment, RMSD, or functional-homology
assessment.
Input Schema
| Name | Required | Description | Default |
|---|---|---|---|
| params | Yes |
Output Schema
| Name | Required | Description | Default |
|---|---|---|---|
No arguments | |||