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DISOPRED3: precise disordered region predictions with annotated protein-binding activity
Author(s) -
David T. Jones,
Domenico Cozzetto
Publication year - 2014
Publication title -
bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.599
H-Index - 390
eISSN - 1367-4811
pISSN - 1367-4803
DOI - 10.1093/bioinformatics/btu744
Subject(s) - intrinsically disordered proteins , computer science , classifier (uml) , sequence (biology) , computational biology , casp , protein methods , support vector machine , identification (biology) , protein structure , data mining , peptide sequence , artificial intelligence , protein structure prediction , biology , genetics , biochemistry , gene , botany
A sizeable fraction of eukaryotic proteins contain intrinsically disordered regions (IDRs), which act in unfolded states or by undergoing transitions between structured and unstructured conformations. Over time, sequence-based classifiers of IDRs have become fairly accurate and currently a major challenge is linking IDRs to their biological roles from the molecular to the systems level.

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