CIDER: Resources to Analyze Sequence-Ensemble Relationships of Intrinsically Disordered Proteins

Intrinsically disordered proteins and regions (IDPs) represent a large class of proteins that are defined by conformational heterogeneity and lack of persistent tertiary/secondary structure. IDPs play important roles in a range of biological functions, and their dysregulation is central to numerous...

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Veröffentlicht in:Biophysical journal 2017-01, Vol.112 (1), p.16-21
Hauptverfasser: Holehouse, Alex S., Das, Rahul K., Ahad, James N., Richardson, Mary O.G., Pappu, Rohit V.
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Sprache:eng
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Zusammenfassung:Intrinsically disordered proteins and regions (IDPs) represent a large class of proteins that are defined by conformational heterogeneity and lack of persistent tertiary/secondary structure. IDPs play important roles in a range of biological functions, and their dysregulation is central to numerous diseases, including neurodegeneration and cancer. The conformational ensembles of IDPs are encoded by their amino acid sequences. Here, we present two computational tools that are designed to enable rapid and high-throughput analyses of a wide range of physicochemical properties encoded by IDP sequences. The first, CIDER, is a user-friendly webserver that enables rapid analysis of IDP sequences. The second, localCIDER, is a high-performance software package that enables a wide range of analyses relevant to IDP sequences. In addition to introducing the two packages, we demonstrate the utility of these resources using examples where sequence analysis offers biophysical insights.
ISSN:0006-3495
1542-0086
DOI:10.1016/j.bpj.2016.11.3200