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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Autores principales:	Crespo, A., Martí, M.A., Estrin, D.A., Roitberg, A.E.
Formato:	JOUR
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:	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

id	todo:paper_00027863_v127_n19_p6940_Crespo
record_format	dspace
spelling	todo:paper_00027863_v127_n19_p6940_Crespo2023-10-03T13:53:42Z Multiple-steering QM-MM calculation of the free energy profile in chorismate mutase Crespo, A. Martí, M.A. Estrin, D.A. Roitberg, A.E. 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 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. Fil:Crespo, A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Martí, M.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Estrin, D.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_00027863_v127_n19_p6940_Crespo
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	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
spellingShingle	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 Crespo, A. Martí, M.A. Estrin, D.A. Roitberg, A.E. Multiple-steering QM-MM calculation of the free energy profile in chorismate mutase
topic_facet	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
description	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.
format	JOUR
author	Crespo, A. Martí, M.A. Estrin, D.A. Roitberg, A.E.
author_facet	Crespo, A. Martí, M.A. Estrin, D.A. Roitberg, A.E.
author_sort	Crespo, A.
title	Multiple-steering QM-MM calculation of the free energy profile in chorismate mutase
title_short	Multiple-steering QM-MM calculation of the free energy profile in chorismate mutase
title_full	Multiple-steering QM-MM calculation of the free energy profile in chorismate mutase
title_fullStr	Multiple-steering QM-MM calculation of the free energy profile in chorismate mutase
title_full_unstemmed	Multiple-steering QM-MM calculation of the free energy profile in chorismate mutase
title_sort	multiple-steering qm-mm calculation of the free energy profile in chorismate mutase
url	http://hdl.handle.net/20.500.12110/paper_00027863_v127_n19_p6940_Crespo
work_keys_str_mv	AT crespoa multiplesteeringqmmmcalculationofthefreeenergyprofileinchorismatemutase AT martima multiplesteeringqmmmcalculationofthefreeenergyprofileinchorismatemutase AT estrinda multiplesteeringqmmmcalculationofthefreeenergyprofileinchorismatemutase AT roitbergae multiplesteeringqmmmcalculationofthefreeenergyprofileinchorismatemutase
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Multiple-steering QM-MM calculation of the free energy profile in chorismate mutase

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