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

Biophys J. 2017 Jan 10;112(1):16-21. doi: 10.1016/j.bpj.2016.11.3200.

Abstract

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.

MeSH terms

  • Computational Biology / methods*
  • Intrinsically Disordered Proteins / chemistry*
  • Models, Molecular
  • Protein Structure, Secondary

Substances

  • Intrinsically Disordered Proteins