ArticleMethods in molecular biology (Clifton, N.J.)2020
Obtaining Hydrodynamic Radii of Intrinsically Disordered Protein Ensembles by Pulsed Field Gradient NMR Measurements.
Article in Methods in molecular biology (Clifton, N.J.), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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6 citing papers in PubMed.
- On the use of dioxane as reference for determination of the hydrodynamic radius by NMR spectroscopy.Biophysical journal · 2024Article
- Design of intrinsically disordered protein variants with diverse structural properties.Science advances · 2024Article
- The molecular basis for cellular function of intrinsically disordered protein regions.Nature reviews. Molecular cell biology · 2024Review
- Design of intrinsically disordered protein variants with diverse structural properties.bioRxiv : the preprint server for biology · 2023Article
- Assessment of models for calculating the hydrodynamic radius of intrinsically disordered proteins.Biophysical journal · 2023Article
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2 authors.
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Abstract
In the disordered state, a protein exhibits a high degree of structural freedom, in both space and time. For an ensemble of disordered or unfolded proteins, this means that the ensemble comprises a high diversity of structures, ranging from compact collapsed states to fully extended polypeptide chains. In addition, each chain is highly dynamic and undergoes conformational changes and local dynamics on both fast and slow timescales. The size properties of disordered proteins are thus best described as ensemble averages. A straightforward measure of the size is the hydrodynamic radius, R
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