ArticleNature communications2022
Temporal and spatial characterisation of protein liquid-liquid phase separation using NMR spectroscopy.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Article
- Liquid-Liquid Phase Separation in Cancer Drug Resistance: Mechanisms and Therapeutic Opportunities.Oncology research · 2026Review
- Beyond structures: solution NMR as the quantitative engine of integrated structural biology.Frontiers in molecular biosciences · 2026Review
- Trifluoroacetic Acid as a Molecular Probe for the Dense Phase in Liquid-Liquid Phase-Separating Peptide Systems.Analytical chemistry · 2025Article
- Continuity of Short-Time Dynamics Crossing the Liquid-Liquid Phase Separation in Charge-Tuned Protein Solutions.The journal of physical chemistry letters · 2024Article
- Accessing self-diffusion on nanosecond time and nanometre length scales with minute kinetic resolution.Journal of applied crystallography · 2024Article
- Decoupling Protein Concentration and Aggregate Content Using Diffusion and Water NMR.Analytical chemistry · 2024Article
- An aberrant fused in sarcoma liquid droplet of amyotrophic lateral sclerosis pathological variant, R495X, accelerates liquid-solid phase transition.Scientific reports · 2024Article
- Multinuclear 1D and 2D NMR withNature communications · 2023Article
- Formation of versus Recruitment to RNA-Rich Condensates: Controlling Effects Exerted by Peptide Side Chain Identity.Journal of the American Chemical Society · 2022Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
Liquid-liquid phase separation (LLPS) of protein solutions is increasingly recognised as an important phenomenon in cell biology and biotechnology. However, opalescence and concentration fluctuations render LLPS difficult to study, particularly when characterising the kinetics of the phase transition and layer separation. Here, we demonstrate the use of a probe molecule trifluoroethanol (TFE) to characterise the kinetics of protein LLPS by NMR spectroscopy. The chemical shift and linewidth of the probe molecule are sensitive to local protein concentration, with this sensitivity resulting in different characteristic signals arising from the dense and lean phases. Monitoring of these probe signals by conventional bulk-detection
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