ArticleInternational journal of molecular sciences2020
New Insight into Mechanisms of Protein Adaptation to High Temperatures: A Comparative Molecular Dynamics Simulation Study of Thermophilic and Mesophilic Subtilisin-Like Serine Proteases.
Article in International journal of molecular sciences, 2020. 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, 34 citations in OpenAlex.
- Identification and Thermal Stability Modification of a Zearalenone Lactone Hydrolase ZHD30L.Toxins · 2026Article
- Molecular Adaptations of Thermophilic Proteins-From Mechanistic Understanding to Machine Learning Approaches.ChemistryOpen · 2026Review
- Structural landscape of bacterial urease: implications for catalyst and adaptation.Archives of microbiology · 2026Review
- Computational Evaluation ofCurrent computer-aided drug design · 2026Article
- Network reorganization of a cold-adapted β-glucosidase couples conformational flexibility to catalytic efficiency under low-temperature conditions.Frontiers in microbiology · 2026Article
- In silico analysis of VP2 protein from infectious bursal disease virus isolate UPM1432/2019: structural dynamics and epitope prediction.Antonie van Leeuwenhoek · 2025Review
- Adaptation of Marine Heterotrophic Protists to Long-Term Warming Selection.Global change biology · 2025Article
- In Silico Analysis of Temperature-Induced Structural, Stability, and Flexibility Modulations in Camel Cytochrome c.Animals : an open access journal from MDPI · 2025Article
- Characterization of a thermostable uricase derived fromFrontiers in microbiology · 2025Article
- Predictive identification and design of potent inhibitors targeting resistance-inducing candidate genes fromFrontiers in bioinformatics · 2024Article
- Host-Pathogen Interactions Influencing Zoonotic Spillover Potential and Transmission in Humans.Viruses · 2023Review
- Review
- Kinetic Modeling, Thermodynamic Approach and Molecular Dynamics Simulation of Thermal Inactivation of Lipases fromInternational journal of molecular sciences · 2022Article
- Effects of the Temperature and Salt Concentration on the Structural Characteristics of the Protein (PDB Code 1BBL).Polymers · 2022Article
- A Minireview on Temperature Dependent Protein Conformational Sampling.The protein journal · 2021Review
- IND-enzymes: a repository for hydrolytic enzymes derived from thermophilic and psychrophilic bacterial species with potential industrial usage.Extremophiles : life under extreme conditions · 2021Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
In high-temperature environments, thermophilic proteins must possess enhanced thermal stability in order to maintain their normal biological functions. However, the physicochemical basis of the structural stability of thermophilic proteins at high temperatures remains elusive. In this study, we performed comparative molecular dynamics simulations on thermophilic serine protease (THM) and its homologous mesophilic counterpart (PRK). The comparative analyses of dynamic structural and geometrical properties suggested that THM adopted a more compact conformation and exhibited more intramolecular interactions and lower global flexibility than PRK, which could be in favor of its thermal stability in high-temperature environments. Comparison between protein solvent interactions and the hydrophobicity of these two forms of serine proteases showed that THM had more burial of nonpolar areas, and less protein solvent hydrogen bonds (HBs), indicating that solvent entropy maximization and mobility may play a significant role in THM's adaption to high temperature environments. The constructed funnel-like free energy landscape (FEL) revealed that, in comparison to PRK, THM had a relatively flat and narrow free energy surface, and a lower minimum free energy level, suggesting that the thermophilic form had lower conformational diversity and flexibility. Combining the FEL theory and our simulation results, we conclude that the solvent (entropy force) plays a significant role in protein adaption at high temperatures.
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