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

被引:11
|
作者
McFadden, William A. [1 ,3 ]
Yanowitz, Judith A. [1 ,2 ]
机构
[1] Womens Res Inst, Pittsburgh, PA 15213 USA
[2] Univ Pittsburgh, Sch Med, Dept Obstet Gynecol & Reprod Sci, Pittsburgh, PA 15260 USA
[3] Emory Univ, Sch Med, Lab Biochem Pharmacol, Atlanta, GA USA
来源
PLOS ONE | 2022年 / 17卷 / 04期
基金
美国国家卫生研究院;
关键词
TUMOR-SUPPRESSOR P53; ALPHA-SYNUCLEIN; HUMAN-DISEASES; DNA-BINDING; SEQUENCE; PREDICTION; MUTATIONS; REGIONS;
D O I
10.1371/journal.pone.0266929
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
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 for Intrinsically Disordered Proteins in R, 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, idpr integrates several amino acid substitution matrices and calculators to supplement IDP-based workflows. Overall, idpr aims to integrate tools for the computational analysis of IDPs within R, facilitating the analysis of these important, yet under-characterized, proteins. The idpr package can be downloaded from Bioconductor(https://bioconductor.org/packages/idpr/).
引用
收藏
页数:12
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