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Highly Abundant Proteins Are Highly Thermostable
Agusto R Luzuriaga-Neira1, Andrew M Ritchie2, Bryan L Payne1
1Biology Department, University of Nevada, Reno, USA.
Genome Biology and Evolution
|July 3, 2023
Summary
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.
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.
Keywords:
expression levelsmisfolding avoidance hypothesisprotein thermostabilityrates of evolutiontranslational robustness hypothesisMore Related Videos
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