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Intrinsically Disordered Proteins Can Behave as Different Polymers across Their Conformational Ensemble.

Saikat Chakraborty1, Tatiana I Morozova2, Jean-Louis Barrat1

  • 1Laboratoire Interdisciplinaire de Physique, Université Grenoble Alpes, CNRS, 38402 Saint-Martin-d'Héres, France.

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Intrinsically disordered proteins (IDPs) exhibit diverse structures. This study reveals beta-casein explores distinct polymer behaviors, from globular to coil-like, depending on its conformational state.

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Area of Science:

  • Biophysics
  • Computational Biology
  • Protein Science

Background:

  • Intrinsically disordered proteins (IDPs) lack stable 3D structures, exploring diverse conformations.
  • Understanding IDP conformational heterogeneity is crucial for their function.

Purpose of the Study:

  • To investigate the conformational space and dynamics of the intrinsically disordered protein beta-casein.
  • To analyze the polymer scaling behavior and structural diversity within different energy funnels.

Main Methods:

  • Hamiltonian replica exchange atomistic molecular dynamics (MD) simulations in explicit water.
  • Analysis of energy landscapes and application of static polymeric scaling laws.
  • Standard MD simulations in the NVT ensemble for representative conformations.

Main Results:

  • Beta-casein's energy landscape features a global minimum and two shallow funnels.
  • Different funnels exhibit distinct polymeric scaling exponents, indicating non-uniform behavior.
  • Conformations near the global minimum are globular, while those near local minima are coil-like.
  • Simulated dynamics show heterogeneous globule-to-coil-like signatures.

Conclusions:

  • IDPs like beta-casein can adopt fundamentally different polymer characteristics in different conformational states.
  • Structural diversity directly impacts the equilibrium dynamics of intrinsically disordered proteins.