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Nucleic Acids Res. 2018 Jul 2;46(W1):W329-W337. doi: 10.1093/nar/gky384.

IUPred2A: context-dependent prediction of protein disorder as a function of redox state and protein binding.

Author information

1
MTA-ELTE Momentum Bioinformatics Research Group, Department of Biochemistry, Eötvös Loránd University, Budapest H-1117, Hungary.

Abstract

The structural states of proteins include ordered globular domains as well as intrinsically disordered protein regions that exist as highly flexible conformational ensembles in isolation. Various computational tools have been developed to discriminate ordered and disordered segments based on the amino acid sequence. However, properties of IDRs can also depend on various conditions, including binding to globular protein partners or environmental factors, such as redox potential. These cases provide further challenges for the computational characterization of disordered segments. In this work we present IUPred2A, a combined web interface that allows to generate energy estimation based predictions for ordered and disordered residues by IUPred2 and for disordered binding regions by ANCHOR2. The updated web server retains the robustness of the original programs but offers several new features. While only minor bug fixes are implemented for IUPred, the next version of ANCHOR is significantly improved through a new architecture and parameters optimized on novel datasets. In addition, redox-sensitive regions can also be highlighted through a novel experimental feature. The web server offers graphical and text outputs, a RESTful interface, access to software download and extensive help, and can be accessed at a new location: http://iupred2a.elte.hu.

PMID:
29860432
PMCID:
PMC6030935
DOI:
10.1093/nar/gky384
[Indexed for MEDLINE]
Free PMC Article

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