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Intrinsically Disordered Protein Ensembles Shape Evolutionary Rates Revealing Conformational Patterns.

Nicolas Palopoli1, Julia Marchetti1, Alexander M Monzon2

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Intrinsically disordered proteins (IDPs) lack stable structures. Evolutionary rates in IDPs correlate with their conformational diversity, offering insights into their dynamic behavior and function.

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Area of Science:

  • Structural Biology
  • Molecular Evolution
  • Biophysics

Background:

  • Intrinsically disordered proteins (IDPs) present challenges in structural biology due to their lack of stable tertiary structure.
  • Their complex dynamics and unique composition necessitate novel approaches for studying their evolution and function.

Purpose of the Study:

  • To investigate the relationship between evolutionary rates and the conformational diversity of intrinsically disordered proteins.
  • To explore how inter-residue contacts influence evolutionary constraints in IDPs.

Main Methods:

  • Utilized Nuclear Magnetic Resonance (NMR) ensembles to analyze protein dynamics.
  • Correlated site-specific evolutionary rate heterogeneity with experimentally observed conformational diversity.
  • Examined the impact of inter-residue contact constraints on evolutionary rates.

Main Results:

  • IDPs exhibit significant site-specific evolutionary rate heterogeneity driven by inter-residue contact constraints.
  • Evolutionary rate profiles align with the conformational diversity of IDPs, suggesting structure-function relationships.
  • Combining a limited set of conformers improved the correlation between evolutionary rates and contact information.

Conclusions:

  • Residue contacts in intrinsically disordered regions constrain evolutionary rates to maintain ensemble dynamics.
  • Evolutionary rates serve as a valuable proxy for assessing the conformational diversity of IDPs.