Springer Protocols: Abstract: Prediction of Intrinsic Disorder and Its Use in Functional Proteomics

Prediction of Intrinsic Disorder and Its Use in Functional Proteomics

By: Vladimir N. Uversky^{2 3}, Predrag Radivojac⁴, Lilia M. Iakoucheva⁵, Zoran Obradovic⁶, A. Keith Dunker²

Abstract

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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.

Affiliation(s): (2) School of Medicine, Indiana University, Indianapolis, IN
(3) Russian Academy of Sciences, Moscow Region, Russia
(4) School of Informatics, Indiana University, Bloomington, IN
(5) The Rockefeller University New York, NY
(6) Temple University, Philadelphia, PA

Book Title: Gene Function Analysis

Series: Methods in Molecular Biology | Volume: 408 | Pub. Date: Aug-23-2007 | Page Range: 69-92 | DOI: 10.1007/978-1-59745-547-3_5

Subject: Genetics/Genomics

Key Words: Intrinsically disordered protein - natively unfolded protein - intrinsically unstructured protein - protein flexibility - disorder prediction - protein function

References

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