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

Lermyte, Frederik (2020)
Roles, Characteristics, and Analysis of Intrinsically Disordered Proteins: A Minireview.
In: Life, 10 (12)
doi: 10.3390/life10120320
Artikel, Bibliographie

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Kurzbeschreibung (Abstract)

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.

Typ des Eintrags: Artikel
Erschienen: 2020
Autor(en): Lermyte, Frederik
Art des Eintrags: Bibliographie
Titel: Roles, Characteristics, and Analysis of Intrinsically Disordered Proteins: A Minireview
Sprache: Englisch
Publikationsjahr: 2020
Verlag: MDPI
Titel der Zeitschrift, Zeitung oder Schriftenreihe: Life
Jahrgang/Volume einer Zeitschrift: 10
(Heft-)Nummer: 12
Kollation: 19 Seiten
DOI: 10.3390/life10120320
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Kurzbeschreibung (Abstract):

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.

Sachgruppe der Dewey Dezimalklassifikatin (DDC): 500 Naturwissenschaften und Mathematik > 540 Chemie
Fachbereich(e)/-gebiet(e): 07 Fachbereich Chemie
07 Fachbereich Chemie > Clemens-Schöpf-Institut > Fachgebiet Biochemie
07 Fachbereich Chemie > Clemens-Schöpf-Institut
Hinterlegungsdatum: 02 Aug 2024 12:35
Letzte Änderung: 02 Aug 2024 12:35
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