Roles, Characteristics, and Analysis of Intrinsically Disordered Proteins: A Minireview

In recent years, there has been a growing understanding that a significant fraction of the eukaryotic proteome is intrinsically disordered, and that these conformationally dynamic proteins play a myriad of vital biological roles in both normal and pathological states. In this review, selected exampl...

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Main Author: Frederik Lermyte
Format: Article
Language:English
Published: MDPI AG 2020-11-01
Series:Life
Subjects:
Online Access:https://www.mdpi.com/2075-1729/10/12/320
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author Frederik Lermyte
author_facet Frederik Lermyte
author_sort Frederik Lermyte
collection DOAJ
description In recent years, there has been a growing understanding that a significant fraction of the eukaryotic proteome is intrinsically disordered, and that these conformationally dynamic proteins play a myriad of vital biological roles in both normal and pathological states. In this review, selected examples of intrinsically disordered proteins are highlighted, with particular attention for a few which are relevant in neurological disorders and in viral infection. Next, the underlying causes for intrinsic disorder are discussed, along with computational methods used to predict whether a given amino acid sequence is likely to adopt a folded or unfolded state in solution. Finally, biophysical methods for the analysis of intrinsically disordered proteins will be discussed, as well as the unique challenges they pose in this context due to their highly dynamic nature.
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spelling doaj.art-96da3a61207a440ebd267326ae1e51322023-11-20T23:01:05ZengMDPI AGLife2075-17292020-11-01101232010.3390/life10120320Roles, Characteristics, and Analysis of Intrinsically Disordered Proteins: A MinireviewFrederik Lermyte0Department of Chemistry, Technical University of Darmstadt, Alarich-Weiss-Straße 4, 64287 Darmstadt, GermanyIn recent years, there has been a growing understanding that a significant fraction of the eukaryotic proteome is intrinsically disordered, and that these conformationally dynamic proteins play a myriad of vital biological roles in both normal and pathological states. In this review, selected examples of intrinsically disordered proteins are highlighted, with particular attention for a few which are relevant in neurological disorders and in viral infection. Next, the underlying causes for intrinsic disorder are discussed, along with computational methods used to predict whether a given amino acid sequence is likely to adopt a folded or unfolded state in solution. Finally, biophysical methods for the analysis of intrinsically disordered proteins will be discussed, as well as the unique challenges they pose in this context due to their highly dynamic nature.https://www.mdpi.com/2075-1729/10/12/320intrinsically disordered proteinstructural biologybiophysicsmass spectrometry
spellingShingle Frederik Lermyte
Roles, Characteristics, and Analysis of Intrinsically Disordered Proteins: A Minireview
Life
intrinsically disordered protein
structural biology
biophysics
mass spectrometry
title Roles, Characteristics, and Analysis of Intrinsically Disordered Proteins: A Minireview
title_full Roles, Characteristics, and Analysis of Intrinsically Disordered Proteins: A Minireview
title_fullStr Roles, Characteristics, and Analysis of Intrinsically Disordered Proteins: A Minireview
title_full_unstemmed Roles, Characteristics, and Analysis of Intrinsically Disordered Proteins: A Minireview
title_short Roles, Characteristics, and Analysis of Intrinsically Disordered Proteins: A Minireview
title_sort roles characteristics and analysis of intrinsically disordered proteins a minireview
topic intrinsically disordered protein
structural biology
biophysics
mass spectrometry
url https://www.mdpi.com/2075-1729/10/12/320
work_keys_str_mv AT frederiklermyte rolescharacteristicsandanalysisofintrinsicallydisorderedproteinsaminireview