Multiple-steering QM-MM calculation of the free energy profile in chorismate mutase

A novel technique for computing free energy profiles in enzymatic reactions using the multiple steering molecular dynamics approach in the context of an efficient QM-MM density functional scheme is presented. The conversion reaction of chorismate to prephenate catalyzed by the Bacillus subtilis enzy...

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Detalles Bibliográficos
Autores principales: Crespo, Alejandro, Martí, Marcelo Adrián, Estrin, Dario Ariel
Publicado: 2005
Materias:
chorismate mutase
article
catalysis
chemical reaction
chemical structure
density functional theory
energy
enthalpy
entropy
enzyme activation
enzyme active site
enzyme activity
molecular mechanics
phase transition
quantum mechanics
Chorismate Mutase
Chorismic Acid
Cyclohexanecarboxylic Acids
Cyclohexenes
Quantum Theory
Thermodynamics
Acceso en línea:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00027863_v127_n19_p6940_Crespo
http://hdl.handle.net/20.500.12110/paper_00027863_v127_n19_p6940_Crespo
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
Descripción
Sumario:A novel technique for computing free energy profiles in enzymatic reactions using the multiple steering molecular dynamics approach in the context of an efficient QM-MM density functional scheme is presented. The conversion reaction of chorismate to prephenate catalyzed by the Bacillus subtilis enzyme chorismate mutase has been chosen as an illustrative example. Copyright © 2005 American Chemical Society.

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