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PMID: 19774619 Published · ppublish English Comparative Study Evaluation Study Journal Article

Assessment of disorder predictions in CASP8.

Proteins ·Vol. 77 Suppl 9 ·2009-00-00 ·Pages 210-6

Noivirt-Brik O, Prilusky J, Sussman JL

Abstract

The interest in intrinsically disordered proteins has greatly increased, as it has become clear that they are very widespread, especially in eukaryotic organisms. Functionally, they appear to play a significant role in the control of many cellular processes and signalling pathways and have been, also, associated with a number of diseases ranging from cancer to Alzheimer's. Thus, there is enormous interest in attempts to predict disordered regions in proteins solely from knowledge of their amino acid sequences. In this study, we assess the quality of predictions for 25 groups on predicting disordered regions in 122 target proteins. In addition, we suggest the need of a "knowledge-independent" measure that would enable one to normalize the results of the different CASP experiments and to determine whether the disorder prediction field had improved across the years.

MeSH Terms
Amino Acid Sequence Computational Biology/methods Models, Molecular Protein Conformation Protein Folding Proteins/chemistry Sequence Analysis, Protein/methods
Chemicals
Proteins
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Noivirt-Brik Orly
Department of Structural Biology, Weizmann Institute of Science, Rehovot 76100, Israel.
Prilusky Jaime
Sussman Joel L
Article Info
Journal
Proteins
Abbr.
Proteins
ISSN
1097-0134
Published
2009-00-00
Pages
210-6
Language
English
Region
United States
NLM ID
8700181
Subset
IM
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