Lermyte, Frederik (2021)
Roles, Characteristics, and Analysis of Intrinsically Disordered Proteins: A Minireview.
In: Life, 2020, 10 (12)
doi: 10.26083/tuprints-00019275
Artikel, Zweitveröffentlichung, Verlagsversion
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: | 2021 |
| Autor(en): | Lermyte, Frederik |
| Art des Eintrags: | Zweitveröffentlichung |
| Titel: | Roles, Characteristics, and Analysis of Intrinsically Disordered Proteins: A Minireview |
| Sprache: | Englisch |
| Publikationsjahr: | 2021 |
| Publikationsdatum der Erstveröffentlichung: | 2020 |
| Verlag: | MDPI |
| Titel der Zeitschrift, Zeitung oder Schriftenreihe: | Life |
| Jahrgang/Volume einer Zeitschrift: | 10 |
| (Heft-)Nummer: | 12 |
| Kollation: | 19 Seiten |
| DOI: | 10.26083/tuprints-00019275 |
| URL / URN: | https://tuprints.ulb.tu-darmstadt.de/19275 |
| Zugehörige Links: | |
| Herkunft: | Zweitveröffentlichung aus gefördertem Golden Open Access |
| 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. |
| Status: | Verlagsversion |
| URN: | urn:nbn:de:tuda-tuprints-192758 |
| 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 |
| Hinterlegungsdatum: | 09 Aug 2021 08:01 |
| Letzte Änderung: | 17 Aug 2021 06:37 |
| PPN: | |
| Zugehörige Links: | |
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| Suche nach Titel in: | TUfind oder in Google |
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