Diversity of hydrodynamic radii of intrinsically disordered proteins.
Conformational change
Fluorescence correlation spectroscopy
Gene expression regulation
Hydrodynamic radius
Intrinsically disordered protein
Journal
European biophysics journal : EBJ
ISSN: 1432-1017
Titre abrégé: Eur Biophys J
Pays: Germany
ID NLM: 8409413
Informations de publication
Date de publication:
Oct 2023
Oct 2023
Historique:
received:
15
05
2023
accepted:
06
09
2023
revised:
08
08
2023
medline:
1
11
2023
pubmed:
13
10
2023
entrez:
13
10
2023
Statut:
ppublish
Résumé
Intrinsically disordered proteins (IDPs) form an important class of biomolecules regulating biological processes in higher organisms. The lack of a fixed spatial structure facilitates them to perform their regulatory functions and allows the efficiency of biochemical reactions to be controlled by temperature and the cellular environment. From the biophysical point of view, IDPs are biopolymers with a broad configuration state space and their actual conformation depends on non-covalent interactions of its amino acid side chain groups at given temperature and chemical conditions. Thus, the hydrodynamic radius (R
Identifiants
pubmed: 37831084
doi: 10.1007/s00249-023-01683-8
pii: 10.1007/s00249-023-01683-8
pmc: PMC10618399
doi:
Substances chimiques
Intrinsically Disordered Proteins
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
607-618Subventions
Organisme : Narodowe Centrum Nauki
ID : UMO-2016/22/E/NZ1/00656
Informations de copyright
© 2023. The Author(s).
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