ArticleEuropean biophysics journal : EBJ2023
Diversity of hydrodynamic radii of intrinsically disordered proteins.
Article in European biophysics journal : EBJ, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 13 citations in OpenAlex.
- Non-Fickian diffusion within assemblies of the intrinsically disordered protein β-casein.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Electrostatic Collapse of Intrinsically Disordered Acid-Rich Protein Is Sensitive to Counterion Valency.The journal of physical chemistry letters · 2025Article
- The C-terminal end of PLIN1 displays structural disorder.Biochemistry and biophysics reports · 2025Article
- The molecular properties of the bHLH TCF4 protein as an intrinsically disordered hub transcription factor.Cell communication and signaling : CCS · 2025Article
- Hydrodynamic Radii of Intrinsically Disordered Proteins: Fast Prediction by Minimum Dissipation Approximation and Experimental Validation.The journal of physical chemistry letters · 2024Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
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
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Registered trials
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