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- W2898511149 abstract "Abstract Enzymes have demonstrated their capacity to acquire thermostability with precise single-residue mutations. We developed a methodology to propose and evaluate stabilizing salt-bridge interactions into the structure of laccase. This oxidoreductase folds into three similar and interacting immunoglobulin-like domains. We identified structural positions prone to strengthen interdomain contacts with a single salt bridge. Ten mutated enzymes were modeled, along with positive and negative controls. We evaluated the mutated structures at three temperatures, with 153 molecular dynamics simulations. Results demonstrated that a computational methodology combining triplicates of molecular dynamics, Poisson-Boltzmann electrostatics and clustering based in principal component analysis, is robust and reliable. Arginine mutants were better than lysine to confer thermostability, and the results indicated that the complex network of interactions in a protein structure requires this type of combined approach to assess the effects of mutations." @default.
- W2898511149 created "2018-11-02" @default.
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- W2898511149 date "2019-01-01" @default.
- W2898511149 modified "2023-10-18" @default.
- W2898511149 title "Molecular dynamics on laccase from Trametes versicolor to examine thermal stability induced by salt bridges" @default.
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- W2898511149 doi "https://doi.org/10.1016/j.chemphys.2018.10.019" @default.
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