ArticleBiophysical journal2011
How do thermophilic proteins and proteomes withstand high temperature?
Article in Biophysical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.
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56 citing papers in PubMed, 148 citations in OpenAlex.
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- Efficient Synthesis of Chemically Recyclable Polyamides via Substituent Effects-Enabled Mechanistic Pathway.Angewandte Chemie (International ed. in English) · 2025Article
- Activation energies of both constructive and destructive cellular biochemistry determine maximum growth temperature in archaea.Communications biology · 2025Article
- A multidomain hydrolase from the thermophile Thermanaeromonas toyohensis degrades high molecular mass forms of polyhydroxybutyrate.Protein science : a publication of the Protein Society · 2025Article
- Arginine: II. Interactions of Its Salt Bridges with Branched Aliphatic Side Chains.The journal of physical chemistry. B · 2025Article
- Exploring the Skin Benefits of Extremophilic Postbiotics fromMicroorganisms · 2025Article
- On Enthalpy-Entropy Compensation Characterizing Processes in Aqueous Solution.Entropy (Basel, Switzerland) · 2025Review
- Protein Quality Control is a Master Modulator of Molecular Evolution in Bacteria.Genome biology and evolution · 2025Review
- Destabilization of the D2 domain of Thermotoga maritima arginine binding protein induced by guanidinium thiocyanate and its counteraction by stabilizing agents.Protein science : a publication of the Protein Society · 2024Article
- The C-terminus is essential for the stability of the mycobacterial channel protein MspA.Protein science : a publication of the Protein Society · 2024Article
- Idiosyncratic genome evolution of the thermophilic cyanobacterium Synechococcus at the limits of phototrophy.The ISME journal · 2024Article
- Homologous Pairs of Low and High Temperature Originating Proteins Spanning the Known Prokaryotic Universe.Scientific data · 2023Article
- The Action of Chemical Denaturants: From Globular to Intrinsically Disordered Proteins.Biology · 2023Review
- Structural Studies of Pif1 Helicases from Thermophilic Bacteria.Microorganisms · 2023Article
- The methanogen core and pangenome: conservation and variability across biology's growth temperature extremes.DNA research : an international journal for rapid publication of reports on genes and genomes · 2023Article
- Diffusive Dynamics of Bacterial Proteome as a Proxy of Cell Death.ACS central science · 2023Article
- Article
- Learning deep representations of enzyme thermal adaptation.Protein science : a publication of the Protein Society · 2022Article
- Some Clues about Enzymes from Psychrophilic Microorganisms.Microorganisms · 2022Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We attempt to understand the origin of enhanced stability in thermophilic proteins by analyzing thermodynamic data for 116 proteins, the largest data set achieved to date. We compute changes in entropy and enthalpy at the convergence temperature where different driving forces are maximally decoupled, in contrast to the majority of previous studies that were performed at the melting temperature. We find, on average, that the gain in enthalpy upon folding is lower in thermophiles than in mesophiles, whereas the loss in entropy upon folding is higher in mesophiles than in thermophiles. This implies that entropic stabilization may be responsible for the high melting temperature, and hints at residual structure or compactness of the denatured state in thermophiles. We find a similar trend by analyzing a homologous set of proteins classified based only on the optimum growth temperature of the organisms from which they were extracted. We find that the folding free energy at the temperature of maximal stability is significantly more favorable in thermophiles than in mesophiles, whereas the maximal stability temperature itself is similar between these two classes. Furthermore, we extend the thermodynamic analysis to model the entire proteome. The results explain the high optimal growth temperature in thermophilic organisms and are in excellent quantitative agreement with full thermal growth rate data obtained in a dozen thermophilic and mesophilic organisms.
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