ArticleBiophysical journal2010
Cellular proteomes have broad distributions of protein stability.
Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.
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Who cites it
52 citing papers in PubMed, 122 citations in OpenAlex.
- Protein Stability, Turnover Kinetics, and Abundance Constrain the Scaling of Protein Interaction Networks.bioRxiv : the preprint server for biology · 2026Article
- ANYI: The ANnotated Yeast Interactome.bioRxiv : the preprint server for biology · 2026Article
- Extreme temperature exposure induces lung-gut dysbiosis in healthy mice.Current research in microbial sciences · 2026Article
- Surface-modified protein crowders influence mutant huntingtin exon 1 aggregation via crowding effects, crowder association, and crowder solution stability.Protein science : a publication of the Protein Society · 2025Article
- Cytoplasmic fluidity and the cold life: proteome stability is decoupled from viability in psychrophiles.Nature communications · 2025Article
- Unifying perspectives on the activity and genotypic targeting of pharmacological chaperones.The Journal of biological chemistry · 2025Review
- Article
- Rapid evolutionary change in trait correlations of single proteins.Nature communications · 2024Article
- When Phased without Water: Biophysics of Cellular Desiccation, from Biomolecules to Condensates.Chemical reviews · 2023Review
- Distribution and solvent exposure of Hsp70 chaperone binding sites across the Escherichia coli proteome.Proteins · 2023Article
- Atomistic simulation of protein evolution reveals sequence covariation and time-dependent fluctuations of site-specific substitution rates.PLoS computational biology · 2023Article
- Diffusive Dynamics of Bacterial Proteome as a Proxy of Cell Death.ACS central science · 2023Article
- The Statistical Trends of Protein Evolution: A Lesson from AlphaFold Database.Molecular biology and evolution · 2022Article
- Genetics of adaptation.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Non-Equilibrium Protein Folding and Activation by ATP-Driven Chaperones.Biomolecules · 2022Article
- Aspects of Biological Replication and Evolution Independent of the Central Dogma: Insights from Protein-Free Vesicular Transformations and Protein-Mediated Membrane Remodeling.The Journal of membrane biology · 2022Article
- A thermodynamic model of protein structure evolution explains empirical amino acid substitution matrices.Protein science : a publication of the Protein Society · 2021Article
- The Protein Folding Problem: The Role of Theory.Journal of molecular biology · 2021Review
- Biophysical and structural studies reveal marginal stability of a crucial hydrocarbon biosynthetic enzyme acyl ACP reductase.Scientific reports · 2021Article
- Chronic temperature stress inhibits reproduction and disrupts endocytosis via chaperone titration in Caenorhabditis elegans.BMC biology · 2021Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
Biological cells are extremely sensitive to temperature. What is the mechanism? We compute the thermal stabilities of the whole proteomes of Escherichia coli, yeast, and Caenorhabditis elegans using an analytical model and an extensive database of stabilities of individual proteins. Our results support the hypothesis that a cell's thermal sensitivities arise from the collective instability of its proteins. This model shows a denaturation catastrophe at temperatures of 49-55°C, roughly the thermal death point of mesophiles. Cells live on the edge of a proteostasis catastrophe. According to the model, it is not that the average protein is problematic; it is the tail of the distribution. About 650 of E. coli's 4300 proteins are less than 4 kcal mol(-1) stable to denaturation. And upshifting by only 4° from 37° to 41°C is estimated to destabilize an average protein by nearly 20%. This model also treats effects of denaturants, osmolytes, and other physical stressors. In addition, it predicts the dependence of cellular growth rates on temperature. This approach may be useful for studying physical forces in biological evolution and the role of climate change on biology.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.