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Agusto R Luzuriaga-Neira1, Andrew M Ritchie2, Bryan L Payne1

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Highly abundant proteins are often more stable and less likely to misfold, supporting the misfolding avoidance hypothesis. This study found that highly expressed proteins generally exhibit greater thermostability, a key prediction of this theory.

Keywords:
expression levelsmisfolding avoidance hypothesisprotein thermostabilityrates of evolutiontranslational robustness hypothesis

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Area of Science:

  • Protein biochemistry
  • Evolutionary biology
  • Computational biology

Background:

  • Highly abundant proteins evolve slowly (E-R anticorrelation).
  • The misfolding avoidance hypothesis links this to toxic effects of misfolded proteins.
  • This hypothesis predicts higher thermostability for abundant proteins.

Purpose of the Study:

  • To computationally investigate the relationship between protein abundance and thermostability.
  • To test the prediction of the misfolding avoidance hypothesis regarding protein expression levels and folding stability.

Main Methods:

  • Comparative analysis of human-mouse orthologous proteins.
  • Utilizing computational methods to assess the free energy of folding (ΔG).
  • Controlling for confounding variables in expression and stability data.

Main Results:

  • A trend was observed where highly expressed orthologs showed a more negative ΔG of folding.
  • This indicates that highly expressed proteins are frequently more thermostable.
  • The effect size was limited, but the trend supported the hypothesis.

Conclusions:

  • The findings support the misfolding avoidance hypothesis.
  • Protein abundance is correlated with increased thermostability, likely to prevent misfolding toxicity.
  • Computational methods provide a robust approach to study protein stability and evolution.