Fig. 2 | Scientific Data

Fig. 2

From: Geometric description of self-interaction potential in symmetric protein complexes

Fig. 2

Workflow used to calculate the ‘environment stickiness’ of a residue illustrated on the dihedral structure of isoaspartyl dipeptidase (PDB accession 1POK). (a) Calculation of the ‘stickiness’ scale. Surface and interface regions are defined for each protein of the dataset4. The stickiness of an amino acid is then defined as the log-ratio of its frequency at protein-protein interfaces relative to solvent-exposed surfaces12. (b) The environment of a residue of interest is defined by surface residues within a 400 Å2 patch centered on the Cα of the residue of interest12. The central residue is excluded from the calculation. (c) Projection of the environment stickiness on isoaspartyl dipeptidase. Residues protected by low interaction propensity environments appear in blue.

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