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Intrinsically disordered proteins (IDPs) form biomolecular condensates. Their chain dynamics, influenced by sequence-specific interactions, predict condensate viscosity and diffusivity, enabling a new framework for understanding and designing these essential cellular structures.

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Area of Science:

  • Biophysics
  • Molecular Biology
  • Soft Matter Physics

Background:

  • Intrinsically disordered proteins (IDPs) are crucial for biomolecular condensate dynamics and material properties.
  • Understanding sequence-property relationships is key for biological function and synthetic design.

Purpose of the Study:

  • Investigate how chain length and charge patterning in model IDPs affect condensate properties.
  • Establish a predictive framework linking molecular sequence to condensate dynamics.

Main Methods:

  • Utilized molecular dynamics simulations for model IDPs with varied chain length and charge patterns.
  • Analyzed chain relaxation times, viscosity, and diffusivity.
  • Compared Rouse and sticky Rouse models for predicting chain dynamics.

Main Results:

  • Chain relaxation times, driven by electrostatic interactions, quantitatively predict condensate viscosity and diffusivity.
  • Condensate dynamics show a crossover between Rouse and reptation behavior.
  • The sticky Rouse model accurately predicts chain reconfiguration and material properties, capturing sequence effects.

Conclusions:

  • Developed a sequence-resolved framework linking molecular interactions to condensate dynamics across scales.
  • Demonstrated that sequence-dependent electrostatic interactions govern condensate viscosity and diffusivity.
  • Provided a predictive model for understanding and designing biomolecular condensates.