HYCUD

The tool HYCUD is described for predicting effective rotational correlation times in multidomain proteins with unstructured tails or linkers, which enable high levels of mobility facilitating their biological function. HYCUD uses hydrodynamic methods and the workflow is demonstrated on the ribosomal protein L7/L12. Predicted correlation times may be used to detect molecular switch events mediated by disorder-order transitions in interdomain linkers.

Topic

Proteins;Protein folds and structural domains;Protein disordered structure;Protein structure analysis

Detail

  • Operation: Protein sequence analysis

  • Software interface: Library

  • Language: Perl;Python

  • License: -

  • Cost: Free

  • Version name: 3.3.1

  • Credit: German Science Foundation Collaborative Research Center, the German Science Foundation research unit

  • Input: -

  • Output: -

  • Contact: Markus Zweckstetter mzwecks@gwdg.de

  • Collection: -

  • Maturity: Stable

Publications

  • HYCUD: a computational tool for prediction of effective rotational correlation time in flexible proteins.
  • Rezaei-Ghaleh N, et al. HYCUD: a computational tool for prediction of effective rotational correlation time in flexible proteins. HYCUD: a computational tool for prediction of effective rotational correlation time in flexible proteins. 2015; 31:1319-21. doi: 10.1093/bioinformatics/btu824
  • https://doi.org/10.1093/bioinformatics/btu824
  • PMID: 25505088
  • PMC: -

Download and documentation

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