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Biophys. J. BioFAST: First Published December 8, 2006. doi:10.1529/biophysj.106.094045
© 2006 by the Biophysical Society.

A more recent version of this article appeared on March 1, 2007.
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PROTEINS

Intrinsic Disorder and Functional Proteomics

Predrag Radivojac 1, Lilia M. Iakoucheva 2, Christopher J. Oldfield 3, Zoran Obradovic 4, Vladimir N Uversky 3* and A. Keith Dunker 5

1 School of Informatics, Indiana University, Bloomington, Indiana, USA
2 Laboratory of Statistical Genetics, The Rockefeller University, New York, New York, USA
3 Indiana University School of Medicine
4 Center for Information Science and Technology, Temple University, Philadelphia, Pennsylvania, USA
5 Indiana University

* To whom correspondence should be addressed. E-mail: uversky{at}chemistry.ucsc.edu.

Submitted on July 26, 2006
Revised on August 30, 2006
Accepted on 15 November 2006


  Abstract
The recent advances in the prediction of intrinsically disordered proteins and the use of protein disorder prediction in the fields of molecular biology and bioinformatics are reviewed here, especially with regard to protein function. First, a close look is taken at intrinsically disordered proteins and then at the methods used for their experimental characterization. Next, the major statistical properties of disordered regions are summarized, and prediction models developed thus far are described, including their numerous applications in functional proteomics. The future of the prediction of protein disorder and the future uses of such predictions in functional proteomics comprise the last section of this article.

Key Words: bioinformatics, intrinsically disordered protein, prediction, protein function, proteomics, unfolded protein




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Copyright © 2006 by the Biophysical Society.