Parallel Computations in the Development of Thermostable Lipase Mutants


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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.

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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Declaração de direitos autorais © Journal of Structural Chemistry, 2018