Proteins & peptides

Hydrophobicity Profile

Sliding-window hydropathy/hydrophobicity profile (ProtScale-style) over a published amino-acid scale. On the Kyte-Doolittle scale it also returns hydrophobicStretches: spans where the 19-residue average stays at or above 1.6, the line Kyte & Doolittle (1982) draw for a membrane-buried segment. ⚠️ That is a FACT ABOUT THE CURVE, not a transmembrane prediction — it cannot tell a signal peptide's h-region from a membrane helix, carries no inside/outside topology, and fires on a buried hydrophobic core in a soluble protein. For an actual prediction use protein_annotate_submit, whose InterProScan run includes Phobius, TMHMM and SignalP.

Batchable via POST /batch.

post/protein_hydrophobicity

Request

  • Base URL: https://seqbench.com/api/v1
  • URL: https://seqbench.com/api/v1/protein_hydrophobicity
  • Auth: none required

Request body

sequencestring required

Protein sequence (one-letter amino-acid codes; non-AA characters ignored).

scale'Kyte-Doolittle' | 'Hopp-Woods' | 'Eisenberg'

Amino-acid scale. Kyte-Doolittle and Eisenberg are hydrophobicity; Hopp-Woods is hydrophilicity.

windowinteger

Sliding-window size (clamped to an odd number ≥ 1). Affects the PROFILE only: hydrophobicStretches is always measured at window 19, because the 1.6 line is calibrated against that window and would otherwise report the plot's smoothing rather than the sequence.

Response

Tool ran successfully.

okunknown required
toolstring required

The tool slug that ran.

resultobject required

Tool-specific output object. Its shape depends on the tool — call GET /{tool} or see the docs for each tool's fields.

Example response

{
  "provenance": {
    "apiVersion": "1.1.0"
  }
}

Changes

No recorded changes to this operation across all 1 revision of this API.