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
相关论文
共 50 条
  • [21] MobiDB: intrinsically disordered proteins in 2021
    Piovesan, Damiano
    Necci, Marco
    Escobedo, Nahuel
    Monzon, Alexander Miguel
    Hatos, Andras
    Micetic, Ivan
    Quaglia, Federica
    Paladin, Lisanna
    Ramasamy, Pathmanaban
    Dosztanyi, Zsuzsanna
    Vranken, Wim F.
    Davey, Norman E.
    Parisi, Gustavo
    Fuxreiter, Monika
    Tosatto, Silvio C. E.
    NUCLEIC ACIDS RESEARCH, 2021, 49 (D1) : D361 - D367
  • [22] Unusual biophysics of intrinsically disordered proteins
    Uversky, Vladimir N.
    BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS, 2013, 1834 (05): : 932 - 951
  • [23] Intrinsically disordered proteins: regulation and disease
    Babu, M. Madan
    van der Lee, Robin
    de Groot, Natalia Sanchez
    Gsponer, Joerg
    CURRENT OPINION IN STRUCTURAL BIOLOGY, 2011, 21 (03) : 432 - 440
  • [24] The importance of the compact disordered state in the fuzzy interactions between intrinsically disordered proteins
    Wang, Dan
    Wu, Shaowen
    Wang, Dongdong
    Song, Xingyu
    Yang, Maohua
    Zhang, Wolun
    Huang, Shaohui
    Weng, Jingwei
    Liu, Zhijun
    Wang, Wenning
    CHEMICAL SCIENCE, 2022, 13 (08) : 2363 - 2377
  • [25] Intrinsically disordered proteins and multicellular organisms
    Dunker, A. Keith
    Bondos, Sarah E.
    Huang, Fei
    Oldfield, Christopher J.
    SEMINARS IN CELL & DEVELOPMENTAL BIOLOGY, 2015, 37 : 44 - 55
  • [26] Intrinsically disordered proteins: administration not executive
    Williamson, Mike P.
    Potts, Jennifer R.
    BIOCHEMICAL SOCIETY TRANSACTIONS, 2012, 40 : 945 - 949
  • [27] Biophysical characterization of intrinsically disordered proteins
    Eliezer, David
    CURRENT OPINION IN STRUCTURAL BIOLOGY, 2009, 19 (01) : 23 - 30
  • [28] Intrinsically disordered proteins in human mitochondria
    Ito, Masahiro
    Tohsato, Yukako
    Sugisawa, Hitoshi
    Kohara, Shohei
    Fukuchi, Satoshi
    Nishikawa, Ikuko
    Nishikawa, Ken
    GENES TO CELLS, 2012, 17 (10) : 817 - 825
  • [29] Fine structures of intrinsically disordered proteins
    Seth, Swarnadeep
    Stine, Brandon
    Bhattacharya, Aniket
    JOURNAL OF CHEMICAL PHYSICS, 2024, 160 (01)
  • [30] Discovery of Cryoprotective Activity in Human Genome-Derived Intrinsically Disordered Proteins
    Matsuo, Naoki
    Goda, Natsuko
    Shimizu, Kana
    Fukuchi, Satoshi
    Ota, Motonori
    Hiroaki, Hidekazu
    INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, 2018, 19 (02)