Parallel Computations in the Development of Thermostable Lipase Mutants
- Autores: Kondratyev M.S.1, Kabanov A.V.1, Samchenko A.A.1, Komarov V.M.1, Khechinashvili N.N.1
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Afiliações:
- Institute of Cell Biophysics
- Edição: Volume 59, Nº 8 (2018)
- Páginas: 1974-1979
- Seção: Article
- URL: https://journals.rcsi.science/0022-4766/article/view/161819
- DOI: https://doi.org/10.1134/S0022476618080292
- ID: 161819
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Resumo
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.
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Sobre autores
M. Kondratyev
Institute of Cell Biophysics
Autor responsável pela correspondência
Email: ma-ko@bk.ru
Rússia, Pushchino
A. Kabanov
Institute of Cell Biophysics
Email: ma-ko@bk.ru
Rússia, Pushchino
A. Samchenko
Institute of Cell Biophysics
Email: ma-ko@bk.ru
Rússia, Pushchino
V. Komarov
Institute of Cell Biophysics
Email: ma-ko@bk.ru
Rússia, Pushchino
N. Khechinashvili
Institute of Cell Biophysics
Email: ma-ko@bk.ru
Rússia, Pushchino
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