ArticleMethods in enzymology2021
Small-angle X-ray scattering experiments of monodisperse intrinsically disordered protein samples close to the solubility limit.
Article in Methods in enzymology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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24 citing papers in PubMed.
- Molecular Insights on the Assembling of ParB1 and ParB1-ACS bio & med chem Au · 2026Article
- The role of the 2'-OH group in phase separation and percolation transitions of RNA.Nature communications · 2026Article
- The Critical Role of the 2'-OH group in Phase Separation and Percolation Transitions of RNA.bioRxiv : the preprint server for biology · 2026Article
- Article
- Beyond structures: solution NMR as the quantitative engine of integrated structural biology.Frontiers in molecular biosciences · 2026Review
- Structural dynamics of IDR interactions in human SFPQ and implications for liquid-liquid phase separation.Acta crystallographica. Section D, Structural biology · 2025Article
- Identifying Sequence Effects on Chain Dimensions of Disordered Proteins by Integrating Experiments and Simulations.JACS Au · 2024Article
- Sequence-dependent conformational preferences of disordered single-stranded RNA.Cell reports. Physical science · 2024Article
- Article
- Cation-induced intramolecular coil-to-globule transition in poly(ADP-ribose).Nature communications · 2024Article
- Design of intrinsically disordered protein variants with diverse structural properties.Science advances · 2024Article
- Article
- The molecular basis for cellular function of intrinsically disordered protein regions.Nature reviews. Molecular cell biology · 2024Review
- Direct prediction of intrinsically disordered protein conformational properties from sequence.Nature methods · 2024Article
- Article
- Structural biases in disordered proteins are prevalent in the cell.Nature structural & molecular biology · 2024Article
- Design of intrinsically disordered protein variants with diverse structural properties.bioRxiv : the preprint server for biology · 2023Article
- Phase separation and molecular ordering of the prion-like domain of the Arabidopsis thermosensory protein EARLY FLOWERING 3.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- The Analytical Flory Random Coil Is a Simple-to-Use Reference Model for Unfolded and Disordered Proteins.The journal of physical chemistry. B · 2023Article
- Recent Advances in NMR Protein Structure Prediction with ROSETTA.International journal of molecular sciences · 2023Review
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Abstract
The condensation of biomolecules into biomolecular condensates via liquid-liquid phase separation (LLPS) is a ubiquitous mechanism that drives cellular organization. To enable these functions, biomolecules have evolved to drive LLPS and facilitate partitioning into biomolecular condensates. Determining the molecular features of proteins that encode LLPS will provide critical insights into a plethora of biological processes. Problematically, probing biomolecular dense phases directly is often technologically difficult or impossible. By capitalizing on the symmetry between the conformational behavior of biomolecules in dilute solution and dense phases, it is possible to infer details critical to phase separation by precise measurements of the dilute phase thus circumventing complicated characterization of dense phases. The symmetry between dilute and dense phases is found in the size and shape of the conformational ensemble of a biomolecule-parameters that small-angle X-ray scattering (SAXS) is ideally suited to probe. Recent technological advances have made it possible to accurately characterize samples of intrinsically disordered protein regions at low enough concentration to avoid interference from intermolecular attraction, oligomerization or aggregation, all of which were previously roadblocks to characterizing self-assembling proteins. Herein, we describe the pitfalls inherent to measuring such samples, the experimental details required for circumventing these issues and analysis methods that place the results of SAXS measurements into the theoretical framework of LLPS.
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