Sequence fingerprints distinguish erroneous from correct predictions of intrinsically disordered protein regions

Konda Mani Saravanan, A. Keith Dunker, Sankaran Krishnaswamy

Research output: Contribution to journalArticle

3 Scopus citations

Abstract

More than 60 prediction methods for intrinsically disordered proteins (IDPs) have been developed over the years, many of which are accessible on the World Wide Web. Nearly, all of these predictors give balanced accuracies in the ~65%–~80% range. Since predictors are not perfect, further studies are required to uncover the role of amino acid residues in native IDP as compared to predicted IDP regions. In the present work, we make use of sequences of 100% predicted IDP regions, false positive disorder predictions, and experimentally determined IDP regions to distinguish the characteristics of native versus predicted IDP regions. A higher occurrence of asparagine is observed in sequences of native IDP regions but not in sequences of false positive predictions of IDP regions. The occurrences of certain combinations of amino acids at the pentapeptide level provide a distinguishing feature in the IDPs with respect to globular proteins. The distinguishing features presented in this paper provide insights into the sequence fingerprints of amino acid residues in experimentally determined as compared to predicted IDP regions. These observations and additional work along these lines should enable the development of improvements in the accuracy of disorder prediction algorithm.

Original languageEnglish (US)
Pages (from-to)4338-4351
Number of pages14
JournalJournal of Biomolecular Structure and Dynamics
Volume36
Issue number16
DOIs
StatePublished - Dec 10 2018

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Keywords

  • dipeptide analysis
  • native intrinsic disorder
  • predicted intrinsic disorder
  • secondary structure prediction
  • sequence fingerprint

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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