Journal of Structural Chemistry

, Volume 59, Issue 8, pp 1974–1979 | Cite as

Parallel Computations in the Development of Thermostable Lipase Mutants

  • M. S. Kondratyev
  • A. V. Kabanov
  • A. A. Samchenko
  • V. M. Komarov
  • N. N. Khechinashvili


The advanced high performance computing methods are used to study the stability and conformational dynamics of the bacterial enzyme lipase LipA, its mutants, and the close homologous enzyme CLE whose substrate is polylactic acid-based plastics. From the analysis of the GPU molecular dynamics of native lipases and their mutants the amino acid residues whose point substitutions can markedly improve the thermostability of the enzymes under study without deteriorating their activity are determined.


lipase LipA CLE thermostability molecular dynamics bioengineering point mutations enzymes 


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Copyright information

© Pleiades Publishing, Ltd. 2018

Authors and Affiliations

  • M. S. Kondratyev
    • 1
  • A. V. Kabanov
    • 1
  • A. A. Samchenko
    • 1
  • V. M. Komarov
    • 1
  • N. N. Khechinashvili
    • 1
  1. 1.Institute of Cell BiophysicsRussian Academy of SciencesPushchinoRussia

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