Gene Function Analysis

Volume 408 of the series Methods in Molecular Biology™ pp 69-92

Prediction of Intrinsic Disorder and Its Use in Functional Proteomics

  • Vladimir N. UverskyAffiliated withSchool of Medicine, Indiana UniversityRussian Academy of Sciences
  • , Predrag RadivojacAffiliated withSchool of Informatics, Indiana University
  • , Lilia M. IakouchevaAffiliated withThe Rockefeller University New York
  • , Zoran ObradovicAffiliated withTemple University
  • , A. Keith DunkerAffiliated withSchool of Medicine, Indiana University

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The number of experimentally verified, intrinsically disordered (ID) proteins is rapidly rising. Research is often focused on a structural characterization of a given protein, looking for several key features. However, ID proteins with their dynamic structures that interconvert on a number of time-scales are difficult targets for the majority of traditional biophysical and biochemical techniques. Structural and functional analyses of these proteins can be significantly aided by disorder predictions. The current advances in the prediction of ID proteins and the use of protein disorder prediction in the fields of molecular biology and bioinformatics are briefly overviewed herein. A method is provided to utilize intrinsic disorder knowledge to gain structural and functional information related to individual proteins, protein groups, families, classes, and even entire proteomes.

Key Words

Intrinsically disordered protein natively unfolded protein intrinsically unstructured protein protein flexibility disorder prediction protein function