Prediction and analysis of intrinsically disordered proteins

Marco Punta, I. Simon, Z. Dosztányi

Research output: Chapter in Book/Report/Conference proceedingChapter

1 Citation (Scopus)

Abstract

Intrinsically disordered proteins and protein regions (IDPs/IDRs) do not adopt a well-defined folded structure under physiological conditions. Instead, these proteins exist as heterogeneous and dynamical conformational ensembles. IDPs are widespread in eukaryotic proteomes and are involved in fundamental biological processes, mostly related to regulation and signaling. At the same time, disordered regions often pose significant challenges to the structure determination process, which generally requires highly homogeneous proteins samples. In this book chapter, we provide a brief overview of protein disorder, describe various bioinformatics resources that have been developed in recent years for their characterization, and give a general outline of their applications in various types of structural genomics projects. Traditionally, disordered segments were filtered out to optimize the yield of structure determination pipelines. However, it is becoming increasingly clear that the structural characterization of proteins cannot be complete without the incorporation of intrinsically disordered regions.

Original languageEnglish
Title of host publicationStructural Proteomics: High-Throughput Methods: Second Edition
PublisherSpringer New York
Pages35-59
Number of pages25
ISBN (Print)9781493922307, 9781493922291
DOIs
Publication statusPublished - Dec 10 2014

Fingerprint

Intrinsically Disordered Proteins
Inosine Diphosphate
Proteins
Biological Phenomena
Proteome
Bioinformatics
Genomics
Computational Biology
Pipelines

Keywords

  • Conformational ensembles
  • Detection of protein disorder
  • Intrinsically unstructured protein
  • Natively unfolded protein
  • Target selection and optimization

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

Cite this

Punta, M., Simon, I., & Dosztányi, Z. (2014). Prediction and analysis of intrinsically disordered proteins. In Structural Proteomics: High-Throughput Methods: Second Edition (pp. 35-59). Springer New York. https://doi.org/10.1007/978-1-4939-2230-7_3

Prediction and analysis of intrinsically disordered proteins. / Punta, Marco; Simon, I.; Dosztányi, Z.

Structural Proteomics: High-Throughput Methods: Second Edition. Springer New York, 2014. p. 35-59.

Research output: Chapter in Book/Report/Conference proceedingChapter

Punta, M, Simon, I & Dosztányi, Z 2014, Prediction and analysis of intrinsically disordered proteins. in Structural Proteomics: High-Throughput Methods: Second Edition. Springer New York, pp. 35-59. https://doi.org/10.1007/978-1-4939-2230-7_3
Punta M, Simon I, Dosztányi Z. Prediction and analysis of intrinsically disordered proteins. In Structural Proteomics: High-Throughput Methods: Second Edition. Springer New York. 2014. p. 35-59 https://doi.org/10.1007/978-1-4939-2230-7_3
Punta, Marco ; Simon, I. ; Dosztányi, Z. / Prediction and analysis of intrinsically disordered proteins. Structural Proteomics: High-Throughput Methods: Second Edition. Springer New York, 2014. pp. 35-59
@inbook{2090197c45734aec866e99a65a104313,
title = "Prediction and analysis of intrinsically disordered proteins",
abstract = "Intrinsically disordered proteins and protein regions (IDPs/IDRs) do not adopt a well-defined folded structure under physiological conditions. Instead, these proteins exist as heterogeneous and dynamical conformational ensembles. IDPs are widespread in eukaryotic proteomes and are involved in fundamental biological processes, mostly related to regulation and signaling. At the same time, disordered regions often pose significant challenges to the structure determination process, which generally requires highly homogeneous proteins samples. In this book chapter, we provide a brief overview of protein disorder, describe various bioinformatics resources that have been developed in recent years for their characterization, and give a general outline of their applications in various types of structural genomics projects. Traditionally, disordered segments were filtered out to optimize the yield of structure determination pipelines. However, it is becoming increasingly clear that the structural characterization of proteins cannot be complete without the incorporation of intrinsically disordered regions.",
keywords = "Conformational ensembles, Detection of protein disorder, Intrinsically unstructured protein, Natively unfolded protein, Target selection and optimization",
author = "Marco Punta and I. Simon and Z. Doszt{\'a}nyi",
year = "2014",
month = "12",
day = "10",
doi = "10.1007/978-1-4939-2230-7_3",
language = "English",
isbn = "9781493922307",
pages = "35--59",
booktitle = "Structural Proteomics: High-Throughput Methods: Second Edition",
publisher = "Springer New York",

}

TY - CHAP

T1 - Prediction and analysis of intrinsically disordered proteins

AU - Punta, Marco

AU - Simon, I.

AU - Dosztányi, Z.

PY - 2014/12/10

Y1 - 2014/12/10

N2 - Intrinsically disordered proteins and protein regions (IDPs/IDRs) do not adopt a well-defined folded structure under physiological conditions. Instead, these proteins exist as heterogeneous and dynamical conformational ensembles. IDPs are widespread in eukaryotic proteomes and are involved in fundamental biological processes, mostly related to regulation and signaling. At the same time, disordered regions often pose significant challenges to the structure determination process, which generally requires highly homogeneous proteins samples. In this book chapter, we provide a brief overview of protein disorder, describe various bioinformatics resources that have been developed in recent years for their characterization, and give a general outline of their applications in various types of structural genomics projects. Traditionally, disordered segments were filtered out to optimize the yield of structure determination pipelines. However, it is becoming increasingly clear that the structural characterization of proteins cannot be complete without the incorporation of intrinsically disordered regions.

AB - Intrinsically disordered proteins and protein regions (IDPs/IDRs) do not adopt a well-defined folded structure under physiological conditions. Instead, these proteins exist as heterogeneous and dynamical conformational ensembles. IDPs are widespread in eukaryotic proteomes and are involved in fundamental biological processes, mostly related to regulation and signaling. At the same time, disordered regions often pose significant challenges to the structure determination process, which generally requires highly homogeneous proteins samples. In this book chapter, we provide a brief overview of protein disorder, describe various bioinformatics resources that have been developed in recent years for their characterization, and give a general outline of their applications in various types of structural genomics projects. Traditionally, disordered segments were filtered out to optimize the yield of structure determination pipelines. However, it is becoming increasingly clear that the structural characterization of proteins cannot be complete without the incorporation of intrinsically disordered regions.

KW - Conformational ensembles

KW - Detection of protein disorder

KW - Intrinsically unstructured protein

KW - Natively unfolded protein

KW - Target selection and optimization

UR - http://www.scopus.com/inward/record.url?scp=84954616522&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84954616522&partnerID=8YFLogxK

U2 - 10.1007/978-1-4939-2230-7_3

DO - 10.1007/978-1-4939-2230-7_3

M3 - Chapter

AN - SCOPUS:84954616522

SN - 9781493922307

SN - 9781493922291

SP - 35

EP - 59

BT - Structural Proteomics: High-Throughput Methods: Second Edition

PB - Springer New York

ER -