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Chemical Dimerization-Induced Protein Condensates on Telomeres

Chemical Dimerization-Induced Protein Condensates on Telomeres

Published on: April 12, 2021

Direct Optical Quantification of Chain Collapse, Reduced Dielectric, and Water Release Driving Protein Phase

Ethan A Perets^1,2, Jacob A Spies¹, Justin H Cheong¹

¹Department of Chemistry, Yale University, New Haven, CT 06520, USA.

Biorxiv : the Preprint Server for Biology

|November 24, 2025

Summary

Biomolecular condensates form via protein chain collapse, driven by reduced water content and dielectric properties. This process, involving the RNA Deadbox helicase 4 (DDX4) protein, enhances interactions and drives condensate growth.

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Area of Science:

Biophysics
Molecular Biology
Cell Biology

Background:

Biomolecular condensates are crucial cellular microenvironments.
Understanding condensate formation requires studying weak, transient interactions.
Investigating condensate interiors is experimentally challenging.

Purpose of the Study:

To investigate the driving forces of biomolecular condensate phase separation.
To determine the structural and chemical properties of condensate interiors.
To elucidate the role of intrinsically disordered proteins in phase separation.

Main Methods:

Combined label-free optical scattering and vibrational spectroscopy (UV, Vis, Mid-IR, Terahertz).
Deep-learning-based prediction of intrinsically disordered protein conformations.
Analysis of RNA Deadbox helicase 4 (DDX4) N-terminal domain behavior.

Main Results:

Intrinsically disordered DDX4 N-terminal domain undergoes chain collapse during phase separation.
Condensate interiors exhibit lower dielectric constants and reduced water content.
Chain collapse, reduced dielectric, and water release strengthen protein-protein interactions.

Conclusions:

DDX4 phase separation is driven by chain collapse and altered solvent properties.
Positive feedback loop involving chain collapse and enhanced interactions drives condensate growth.
Provides quantitative insights into protein-protein/protein-solvent interactions within condensates.