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• W3023544438 startingPage "3128" @default.
• W3023544438 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." @default.
• W3023544438 created "2020-05-13" @default.
• W3023544438 creator A5029697012 @default.
• W3023544438 creator A5088523149 @default.
• W3023544438 creator A5091692295 @default.
• W3023544438 date "2020-04-28" @default.
• W3023544438 modified "2023-09-29" @default.
• W3023544438 title "New Insight into Mechanisms of Protein Adaptation to High Temperatures: A Comparative Molecular Dynamics Simulation Study of Thermophilic and Mesophilic Subtilisin-Like Serine Proteases" @default.
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• W3023544438 doi "https://doi.org/10.3390/ijms21093128" @default.
• W3023544438 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/7247438" @default.
• W3023544438 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/32354206" @default.
• W3023544438 hasPublicationYear "2020" @default.
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