Molecular dynamics simulations of active site mutants of rat liver arginase

By using molecular dynamics (MD) simulations and crystallographic data for rat liver arginase, the substrate positions in the active sites of native and mutant forms of the enzyme, were compared and correlated with known kinetic consequences of mutations. The mutants compared were His 141<IMG SRC...

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Autores principales: Canales,Mauricio, Westermeyer,Linda, Carvajal,Nelson
Lenguaje:English
Publicado: Pontificia Universidad Católica de Valparaíso 2001
Acceso en línea:http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582001000300010
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