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Thermostability of Enzymes from Molecular Dynamics Simulations.

ABSTRACT: Thermodynamic stability is a central requirement for protein function, and one goal of protein engineering is improvement of stability, particularly for applications in biotechnology. Herein, molecular dynamics simulations are used to predict in vitro thermostability of members of the bacterial ribonuclease HI (RNase H) family of endonucleases. The temperature dependence of the generalized order parameter, S, for four RNase H homologues, from psychrotrophic, mesophilic, and thermophilic organisms, is highly correlated with experimentally determined melting temperatures and with calculated free energies of folding at the midpoint temperature of the simulations. This study provides an approach for in silico mutational screens to improve thermostability of biologically and industrially relevant enzymes.

SUBMITTER: Zeiske T 

PROVIDER: S-EPMC4977845 | biostudies-literature | 2016 Jun

REPOSITORIES: biostudies-literature

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Thermostability of Enzymes from Molecular Dynamics Simulations.

Zeiske Tim T   Stafford Kate A KA   Palmer Arthur G AG  

Journal of chemical theory and computation 20160506 6

Thermodynamic stability is a central requirement for protein function, and one goal of protein engineering is improvement of stability, particularly for applications in biotechnology. Herein, molecular dynamics simulations are used to predict in vitro thermostability of members of the bacterial ribonuclease HI (RNase H) family of endonucleases. The temperature dependence of the generalized order parameter, S, for four RNase H homologues, from psychrotrophic, mesophilic, and thermophilic organism  ...[more]

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