The effect of active-site isoleucine to alanine mutation on the DHFR catalyzed hydride-transfer

Comparison of the nature of hydride transfer in wild-type and active site mutant (I14A) of dihydrofolate reductase suggests that the size of this side chain at position 14 modulates H-tunneling. © 2010 The Royal Society of Chemistry.

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Detalles Bibliográficos
Publicado:	2010
Materias:	alanine dihydrofolate reductase hydrogen isoleucine article biotransformation catalysis chemical reaction crystal structure molecular dynamics quantum mechanics site directed mutagenesis synthesis Alanine Amino Acid Substitution Catalysis Catalytic Domain Escherichia coli Isoleucine Kinetics Molecular Dynamics Simulation Mutation NADP Tetrahydrofolate Dehydrogenase
Acceso en línea:	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_13597345_v46_n47_p8974_Stojković http://hdl.handle.net/20.500.12110/paper_13597345_v46_n47_p8974_Stojković
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	paper:paper_13597345_v46_n47_p8974_StojkoviÃÂ
record_format	dspace
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	alanine dihydrofolate reductase hydrogen isoleucine article biotransformation catalysis chemical reaction crystal structure molecular dynamics quantum mechanics site directed mutagenesis synthesis Alanine Amino Acid Substitution Catalysis Catalytic Domain Escherichia coli Isoleucine Kinetics Molecular Dynamics Simulation Mutation NADP Tetrahydrofolate Dehydrogenase
spellingShingle	alanine dihydrofolate reductase hydrogen isoleucine article biotransformation catalysis chemical reaction crystal structure molecular dynamics quantum mechanics site directed mutagenesis synthesis Alanine Amino Acid Substitution Catalysis Catalytic Domain Escherichia coli Isoleucine Kinetics Molecular Dynamics Simulation Mutation NADP Tetrahydrofolate Dehydrogenase The effect of active-site isoleucine to alanine mutation on the DHFR catalyzed hydride-transfer
topic_facet	alanine dihydrofolate reductase hydrogen isoleucine article biotransformation catalysis chemical reaction crystal structure molecular dynamics quantum mechanics site directed mutagenesis synthesis Alanine Amino Acid Substitution Catalysis Catalytic Domain Escherichia coli Isoleucine Kinetics Molecular Dynamics Simulation Mutation NADP Tetrahydrofolate Dehydrogenase
description	Comparison of the nature of hydride transfer in wild-type and active site mutant (I14A) of dihydrofolate reductase suggests that the size of this side chain at position 14 modulates H-tunneling. © 2010 The Royal Society of Chemistry.
title	The effect of active-site isoleucine to alanine mutation on the DHFR catalyzed hydride-transfer
title_short	The effect of active-site isoleucine to alanine mutation on the DHFR catalyzed hydride-transfer
title_full	The effect of active-site isoleucine to alanine mutation on the DHFR catalyzed hydride-transfer
title_fullStr	The effect of active-site isoleucine to alanine mutation on the DHFR catalyzed hydride-transfer
title_full_unstemmed	The effect of active-site isoleucine to alanine mutation on the DHFR catalyzed hydride-transfer
title_sort	effect of active-site isoleucine to alanine mutation on the dhfr catalyzed hydride-transfer
publishDate	2010
url	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_13597345_v46_n47_p8974_Stojković http://hdl.handle.net/20.500.12110/paper_13597345_v46_n47_p8974_Stojković
bdutipo_str	Repositorios
_version_	1764820567655972866

The effect of active-site isoleucine to alanine mutation on the DHFR catalyzed hydride-transfer

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