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Updated: Aug 5, 2026
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Using Solution NMR to Characterize Biomolecular Condensates Under Biphasic Conditions
Published on: April 17, 2026
From Pan-Life Phase Insights to PhaseHub: Analyzing Protein Condensate Complexity
Qiyu Liang1, Weibo Gao2, Yansong Miao3
1School of Physical and Mathematical Sciences, Nanyang Technological University, 637371, Singapore; School of Biological Sciences, Nanyang Technological University, 637551, Singapore.
Molecular Plant
|July 30, 2026
Summary
Biomolecular condensates form essential signaling hubs. This study reveals how phase separation evolves across species, balancing function and aggregation, and introduces PhaseHub for exploring these dynamic systems.
Area of Science:
- Cell Biology
- Evolutionary Biology
- Biophysics
Background:
- Intracellular biomolecular condensation creates signaling hubs crucial for cellular processes.
- Understanding the dynamic organization of these multicomponent, far-from-equilibrium systems is challenging.
Purpose of the Study:
- To analyze phase separation (PS) proteins across the Tree of Life.
- To investigate the evolutionary mechanisms governing phase separation.
- To develop a framework and resource for studying signaling hubs.
Main Methods:
- Computational analysis of PS proteins in 1,106 species.
- Examination of amino acid homorepeat-containing proteins (HRPs).
- Integration of PS propensity with experimental data (abundance, interactomes, localization) in model eukaryotes.
- Development of the PhaseHub web interface.
Main Results:
- Eukaryotes show higher PS propensity than prokaryotes, influenced by genome size.
- Phase separation evolution balances functional condensation with aggregation avoidance.
- Potential signaling hubs and components were identified across kingdoms.
- PhaseHub provides a platform for exploring PS dynamics and components.
Conclusions:
- An evolutionary framework integrating molecular grammar and physiological context aids understanding of multicomponent PS hubs.
- The study facilitates hypothesis generation and rational design of biomolecular condensates.
