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Sequence Effects on Size, Shape, and Structural Heterogeneity in Intrinsically Disordered Proteins.

Upayan Baul1, Debayan Chakraborty1, Mauro L Mugnai1

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Intrinsically disordered proteins (IDPs) explore diverse structures, challenging polymer scaling laws. Sequence, not just length, dictates their conformational heterogeneity, crucial for cellular functions.

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Area of Science:

  • Biophysics
  • Structural Biology
  • Computational Biology

Background:

  • Intrinsically disordered proteins (IDPs) lack stable 3D structures, complicating structure-function relationship studies.
  • Understanding the conformational ensemble of IDPs is key to elucidating their diverse cellular roles.

Purpose of the Study:

  • To quantitatively characterize IDP structural features based on sequence and length.
  • To investigate the relationship between IDP sequence, conformational diversity, and ensemble-averaged properties.

Main Methods:

  • Utilized coarse-grained simulations to model IDPs of varying lengths (20-441 residues).
  • Performed clustering analysis to assess conformational heterogeneity.
  • Validated simulation results against experimental data, including radii of gyration and small-angle X-ray scattering profiles.

Main Results:

  • Simulations accurately reproduced experimental radii of gyration and scattering profiles for diverse IDP sequences.
  • IDP ensemble-averaged properties align with Flory scaling laws (ν ≈ 0.588), suggesting good solvent polymer behavior.
  • Clustering analysis revealed significant sequence-dependent conformational heterogeneity, contradicting simple polymer models. Compact conformations were observed even for charged IDPs like Prothymosin-α.
  • Similar sequences (α-Synuclein, Tau fragment) exhibited distinct conformational heterogeneity.

Conclusions:

  • IDP structural behavior is highly sequence-specific, with significant conformational diversity beyond ensemble-averaged properties.
  • Simple metrics like net charge are insufficient to predict IDP phase behavior.
  • This study provides a foundation for exploring IDP interactions in cellular contexts like stress granules and biomolecular condensates.