HCAtk and pyHCA: A Toolkit and Python API for the Hydrophobic Cluster Analysis of Protein Sequences

Tristan Bitard-Feildel; Isabelle Callebaut

The second example concerns a disordered region (amino acids 82 to 134) found in another member protein has a high degree of intrinsic disorder, as revealed by the experimental NMR structure of the full 164 length protein, without truncation of the N-or C-terminal regions [15] . No clear function is currently 165 associated with the N-and C-terminal regions of the protein. As for the previous example, the HCA 166 pattern displayed by the disordered region is similar to patterns observed for foldable regions, suggesting 167 that this small domain is able to fold, at least under particular conditions. The copyright holder for this preprint (which was not peer-reviewed) is the author/funder. It . https://doi.org/10.1101/249995 doi: bioRxiv preprint Figure S6 : Disordered regions with high HCA score -example n o 2. The HCA pattern displayed by this disordered region is similar to pattern of foldable regions. Clusters of several hydrophobic residues can be seen close together. The disordered region, (82-134) corresponds to the C-terminal of human Zinc finger protein 593 (UniProt O00488).