ArticleBiophysical journal2002
Toward the physical basis of thermophilic proteins: linking of enriched polar interactions and reduced heat capacity of unfolding.
Article in Biophysical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- Global analysis of thermal and chemical denaturation using CheMelt: Thermodynamic dissection of highly thermostable de novo designed proteins.Protein science : a publication of the Protein Society · 2026Article
- Genomic, Proteomic, and Structural Insights Into the Transition of FtsZ From Thermophiles to Mesophiles Across the Prokaryotic Kingdom.Proteins · 2026Article
- Exploring the Skin Benefits of Extremophilic Postbiotics fromMicroorganisms · 2025Article
- Engineering enhanced thermostability into theCurrent research in structural biology · 2022Article
- Consensus protein engineering on the thermostable histone-like bacterial protein HUs significantly improves stability and DNA binding affinity.Extremophiles : life under extreme conditions · 2020Article
- Electrostatic Interactions in Protein Structure, Folding, Binding, and Condensation.Chemical reviews · 2018Review
- Role of Proteome Physical Chemistry in Cell Behavior.The journal of physical chemistry. B · 2016Review
- Electrostatic effects on the folding stability of FKBP12.Protein engineering, design & selection : PEDS · 2016Article
- How conformational flexibility stabilizes the hyperthermophilic elongation factor G-domain.The journal of physical chemistry. B · 2013Article
- Thermophilic proteins: insight and perspective from in silico experiments.Chemical Society reviews · 2012Review
- How do thermophilic proteins and proteomes withstand high temperature?Biophysical journal · 2011Article
- Stabilizing salt-bridge enhances protein thermostability by reducing the heat capacity change of unfolding.PloS one · 2011Article
- Increasing protein stability: importance of DeltaC(p) and the denatured state.Protein science : a publication of the Protein Society · 2010Article
- Temperature dependence of the flexibility of thermophilic and mesophilic flavoenzymes of the nitroreductase fold.Protein engineering, design & selection : PEDS · 2010Article
- Computing protein stabilities from their chain lengths.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Explanation of the stability of thermophilic proteins based on unique micromorphology.Biophysical journal · 2006Article
- Conformational flexibility revealed by the crystal structure of a crenarchaeal RadA.Nucleic acids research · 2005Article
- Stabilizing roles of residual structure in the empty heme binding pockets and unfolded states of microsomal and mitochondrial apocytochrome b5.Protein science : a publication of the Protein Society · 2004Article
- Entropy-driven folding of an RNA helical junction: an isothermal titration calorimetric analysis of the hammerhead ribozyme.Biochemistry · 2004Article
- Comparison of calculation and experiment implicates significant electrostatic contributions to the binding stability of barnase and barstar.Biophysical journal · 2003Article
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1 author.
Funding
Abstract
The enrichment of salt bridges and hydrogen bonding in thermophilic proteins has long been recognized. Another tendency, featuring lower heat capacity of unfolding (DeltaC(p)) than found in mesophilic proteins, is emerging from the recent literature. Here we present a simple electrostatic model to illustrate that formation of a salt-bridge or hydrogen-bonding network around an ionized group in the folded state leads to increased folding stability and decreased DeltaC(p). We thus suggest that the reduced DeltaC(p) of thermophilic proteins could partly be attributed to enriched polar interactions. A reduced DeltaC(p) might serve as an indicator for the contribution of polar interactions to folding stability.
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