idpr: A package for profiling and analyzing Intrinsically Disordered Proteins in R

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Abstract
Intrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDRs) are proteins or protein-domains that do not have a single native structure, rather, they are a class of flexible peptides that can rapidly adopt multiple conformations. IDPs are quite abundant, and their dynamic characteristics provide unique advantages for various biological processes. The field of “unstructured biology” has emerged, in part, because of numerous computational studies that had identified the unique characteristics of IDPs and IDRs. The package ‘idpr’, short forIntrinsicallyDisorderedProteins inR, implements several R functions that match the established characteristics of IDPs to protein sequences of interest. This includes calculations of residue composition, charge-hydropathy relationships, and predictions of intrinsic disorder. Additionally,idprintegrates several amino acid substitution matrices and calculators to supplement IDP-based workflows. Overall,idpraims to integrate tools for the computational analysis of IDPs within R, facilitating the analysis of these important, yet under-characterized, proteins. Theidprpackage can be downloaded from Bioconductor (https://bioconductor.org/packages/idpr/).
Funding Information
  • National Institute of General Medical Sciences (R01GM127569)

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