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Backbone rigidity encodes universal viscoelastic signatures in biomolecular condensates
Sean Yang1, Subhadip Biswas1, Davit A Potoyan2
1Department of Chemistry, Iowa State University, Ames Iowa.
Biophysical Journal
|February 6, 2026
Summary
Sequence-dependent chain rigidity in intrinsically disordered proteins explains the viscoelasticity of biomolecular condensates. This finding advances our understanding of condensate behavior and its sequence-encoded properties.
Area of Science:
- Biophysics
- Soft Matter Physics
- Computational Biology
Background:
- Biomolecular condensates display diverse viscoelastic properties influenced by molecular composition.
- Coarse-grained models of intrinsically disordered proteins (IDPs) are crucial for understanding condensate structure and thermodynamics.
- Standard flexible chain models often fail to capture the complex viscoelasticity of IDPs, predicting only viscous behavior.
Purpose of the Study:
- To investigate the role of sequence-dependent chain rigidity in accurately modeling the viscoelastic properties of biomolecular condensates.
- To develop a coarse-grained model that reproduces experimentally observed elastic and viscous moduli.
- To identify descriptors for characterizing condensate viscoelasticity and explore sequence-structure-property relationships.
Main Methods:
- Development and application of a single-bead, semiflexible coarse-grained model for intrinsically disordered proteins.
- Simulation of A1-LCD condensates and their variants to analyze viscoelastic properties.
- Characterization of frequency-dependent loss factors and correlation with viscosity.
- Investigation of the impact of backbone rigidity on condensate conformation and dynamics.
Main Results:
- Introducing sequence-dependent chain rigidity successfully reproduces experimentally observed elastic and viscous moduli for A1-LCD condensates.
- A single descriptor effectively characterizes the frequency-dependent loss factor, correlating with viscosity across different A1-LCD variants.
- Increased backbone rigidity leads to more extended condensate conformations and an expanded elastic-dominated frequency range.
- Sequence rearrangements promoting sticker clusters were identified as a mechanism for tuning viscoelasticity.
Conclusions:
- Sequence-dependent chain rigidity is essential for accurately modeling the viscoelastic behavior of biomolecular condensates formed by IDPs.
- The developed coarse-grained model provides a powerful tool for predicting and understanding condensate properties.
- Viscoelasticity in condensates is intrinsically encoded in the protein sequence and can be modulated through specific sequence designs.
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