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Decoding Biomolecular Condensate Dynamics: An Energy Landscape Approach.

Subhadip Biswas, Davit A Potoyan

    Biorxiv : the Preprint Server for Biology
    |October 10, 2024
    PubMed
    Summary

    Protein low-complexity sequences form biomolecular condensates. Their patterns dictate material properties, with periodic sequences promoting elasticity and random ones viscosity, preventing pathological states.

    Area of Science:

    • Biochemistry
    • Biophysics
    • Molecular Biology

    Background:

    • Eukaryotic proteins often feature low-complexity sequence (LCS) elements with poorly understood roles.
    • These LCS regions can form dynamic biomolecular condensates, crucial for cellular processes.
    • Mutations in LCS can lead to aberrant phase transitions, forming pathological solid-like states.

    Purpose of the Study:

    • To elucidate how LCS patterns encode the material properties of protein condensates.
    • To understand the functional and evolutionary significance of LCS in proteins.

    Main Methods:

    • Utilized an alphabet-free energy landscape framework based on 'stickers' and 'spacers'.
    • Analyzed the relationship between LCS sequence patterns and condensate material properties.

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    Main Results:

    • Identified a phase diagram of material properties governed by energy landscape features.
    • Periodic repeat motifs in LCS correlate with elastic-dominated condensate properties.
    • Random sequences in LCS are associated with viscous-dominated properties.
    • A specific degree of sticker periodicity is essential for maintaining condensate fluidity and preventing solid-like states.

    Conclusions:

    • The energy landscape framework effectively deciphers the encoding of condensate properties by LCS patterns.
    • Findings reveal how sequence periodicity influences condensate viscoelasticity, offering insights into disease mechanisms.
    • The framework predicts how altering sticker periodicity and strength can modulate protein condensate viscoelasticity.