ArticleBiophysical journal2006
Similarity and difference in the unfolding of thermophilic and mesophilic cold shock proteins studied by molecular dynamics simulations.
Article in Biophysical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Effect of Additional Terminal Residues on the Folding and Unfolding Dynamics of Cold Shock Protein.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Understanding thermal and organic solvent stability of thermoalkalophilic lipases: insights from computational predictions and experiments.Journal of molecular modeling · 2020Article
- Electrostatic Interactions in Protein Structure, Folding, Binding, and Condensation.Chemical reviews · 2018Review
- Improving the thermal stability of cellobiohydrolase Cel7A fromThe Journal of biological chemistry · 2017Article
- Terahertz Frequency Spectroscopy to Determine Cold Shock Protein Stability upon Solvation and Evaporation - A Molecular Dynamics Study.IEEE transactions on terahertz science and technology · 2017Article
- Role of Proteome Physical Chemistry in Cell Behavior.The journal of physical chemistry. B · 2016Review
- Effect of Mutation and Substrate Binding on the Stability of Cytochrome P450BM3 Variants.Biochemistry · 2016Article
- Impacts of the charged residues mutation S48E/N62H on the thermostability and unfolding behavior of cold shock protein: insights from molecular dynamics simulation with Gō model.Journal of molecular modeling · 2016Article
- Physicochemical Properties of Ion Pairs of Biological Macromolecules.Biomolecules · 2015Review
- How conformational flexibility stabilizes the hyperthermophilic elongation factor G-domain.The journal of physical chemistry. B · 2013Article
- Is there an en route folding intermediate for Cold shock proteins?Protein science : a publication of the Protein Society · 2012Article
- Using molecular dynamics to probe the structural basis for enhanced stability in thermal stable cytochromes P450.Biochemistry · 2010Article
- The folding transition-state ensemble of a four-helix bundle protein: helix propensity as a determinant and macromolecular crowding as a probe.Biophysical journal · 2010Article
- Temperature dependence of the flexibility of thermophilic and mesophilic flavoenzymes of the nitroreductase fold.Protein engineering, design & selection : PEDS · 2010Article
- Atomistic modeling of macromolecular crowding predicts modest increases in protein folding and binding stability.Biophysical journal · 2009Article
- Fundamental aspects of protein-protein association kinetics.Chemical reviews · 2009Review
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Authors and funding
2 authors.
Funding
Abstract
Molecular dynamics simulations were performed to unfold a homologous pair of thermophilic and mesophilic cold shock proteins at high temperatures. The two proteins differ in just 11 of 66 residues and have very similar structures with a closed five-stranded antiparallel beta-barrel. A long flexible loop connects the N-terminal side of the barrel, formed by three strands (beta1-beta3), with the C-terminal side, formed by two strands (beta4-beta5). The two proteins were found to follow the same unfolding pathway, but with the thermophilic protein showing much slower unfolding. Unfolding started with the melting of C-terminal strands, leading to exposure of the hydrophobic core. Subsequent melting of beta3 and the beta-hairpin formed by the first two strands then resulted in unfolding of the whole protein. The slower unfolding of the thermophilic protein could be attributed to ion pair formation of Arg-3 with Glu-46, Glu-21, and the C-terminal. These ion pairs were also found to be important for the difference in folding stability between the pair of proteins. Thus electrostatic interactions appear to play similar roles in the difference in folding stability and kinetics between the pair of proteins.
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