CIDER: Resources to Analyze Sequence-Ensemble Relationships of Intrinsically Disordered Proteins
Washington University in St. Louis · Living Systems (United States)
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,…
Citation impact
- FWCI
- 14.69
- Percentile
- 100%
- References
- 48
Authors
5- ASAlex S. HolehouseCorresponding
Washington University in St. Louis, Living Systems (United States)
- RKRahul K. Das
Washington University in St. Louis
- JAJames Ahad
Washington University in St. Louis
- MOMary O.G. Richardson
Washington University in St. Louis
- RVRohit V. Pappu
Washington University in St. Louis, Living Systems (United States)
Topics & keywords
- Intrinsically disordered proteins
- Computational biology
- Sequence (biology)
- Conformational ensembles
- Computer science
- Biology
- Range (aeronautics)
- Protein secondary structure