Unraveling the role of protein dynamics in dihydrofolate reductase catalysis
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Dispelling the effects of a sorceress in enzyme catalysisThe importance of ensemble averaging in enzyme kineticsEnzyme dynamics from NMR spectroscopyTriple Isotope Effects Support Concerted Hydride and Proton Transfer and Promoting Vibrations in Human Heart Lactate DehydrogenaseDoes the pressure dependence of kinetic isotope effects report usefully on dynamics in enzyme H-transfer reactions?Chemical Ligation and Isotope Labeling to Locate Dynamic Effects during Catalysis by Dihydrofolate ReductasePerspective: Defining and quantifying the role of dynamics in enzyme catalysisComparison of the Internal Dynamics of Metalloproteases Provides New Insights on Their Function and Evolution.How Accurate Are Transition States from Simulations of Enzymatic Reactions?Comparative laboratory evolution of ordered and disordered enzymes.Transition States and transition state analogue interactions with enzymes.Cofactor-Mediated Conformational Dynamics Promote Product Release From Escherichia coli Dihydrofolate Reductase via an Allosteric Pathway.Linking protein motion to enzyme catalysis.Hydride Transfer in DHFR by Transition Path Sampling, Kinetic Isotope Effects, and Heavy Enzyme StudiesThe Effect of Protein Mass Modulation on Human Dihydrofolate Reductase.Liberation of H2 from (o-C6H4Me)3P-H(+) + (-)H-B(p-C6F4H)3 ion-pair: A transition-state in the minimum energy path versus the transient species in Born-Oppenheimer molecular dynamics.Extension and limits of the network of coupled motions correlated to hydride transfer in dihydrofolate reductase.Atom Tunneling in Chemistry.Dynamic and Electrostatic Effects on the Reaction Catalyzed by HIV-1 Protease.Applications of NMR and computational methodologies to study protein dynamics.Preserved hydride transfer mechanism in evolutionarily divergent thymidylate synthases.Different dynamical effects in mesophilic and hyperthermophilic dihydrofolate reductases.Protein mass-modulated effects in the catalytic mechanism of dihydrofolate reductase: beyond promoting vibrations.Examinations of the Chemical Step in Enzyme Catalysis.Pinpointing dynamic coupling in enzymes for efficient drug design.Increased dynamic effects in a catalytically compromised variant of Escherichia coli dihydrofolate reductase.Simulations of remote mutants of dihydrofolate reductase reveal the nature of a network of residues coupled to hydride transfer.Are there dynamical effects in enzyme catalysis? Some thoughts concerning the enzymatic chemical step.How frustrated Lewis acid/base systems pass through transition-state regions: H2 cleavage by [tBu3P/B(C6F5)3].Quantifying the limits of transition state theory in enzymatic catalysis.Isotope Substitution of Promiscuous Alcohol Dehydrogenase Reveals the Origin of Substrate Preference in the Transition State.Adaptive free energy sampling in multidimensional collective variable space using boxed molecular dynamics.Change in heat capacity accurately predicts vibrational coupling in enzyme catalyzed reactions.The role of the Met20 loop in the hydride transfer in Escherichia coli dihydrofolate reductase.Promoting Vibrations and the Function of Enzymes. Emerging Theoretical and Experimental Convergence.Dynamical origins of heat capacity changes in enzyme-catalysed reactions.Protein motions and dynamic effects in enzyme catalysis.Direct observation of ultrafast large-scale dynamics of an enzyme under turnover conditions.Minimization of dynamic effects in the evolution of dihydrofolate reductase† †Electronic supplementary information (ESI) available: Full experimental procedures; mass spectra of purified proteins; circular dichroism spectra, tabulated experimental dDer Tunneleffekt von Atomen in der Chemie
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Unraveling the role of protein dynamics in dihydrofolate reductase catalysis
description
article científic
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article scientifique
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articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 24 September 2013
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vedecký článok
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vetenskaplig artikel
@sv
videnskabelig artikel
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vědecký článek
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name
Unraveling the role of protein dynamics in dihydrofolate reductase catalysis
@en
Unraveling the role of protein dynamics in dihydrofolate reductase catalysis.
@nl
type
label
Unraveling the role of protein dynamics in dihydrofolate reductase catalysis
@en
Unraveling the role of protein dynamics in dihydrofolate reductase catalysis.
@nl
prefLabel
Unraveling the role of protein dynamics in dihydrofolate reductase catalysis
@en
Unraveling the role of protein dynamics in dihydrofolate reductase catalysis.
@nl
P2093
P2860
P50
P356
P1476
Unraveling the role of protein dynamics in dihydrofolate reductase catalysis
@en
P2093
David R Glowacki
J Javier Ruiz-Pernía
Rudolf K Allemann
P2860
P304
16344-16349
P356
10.1073/PNAS.1312437110
P407
P50
P577
2013-09-24T00:00:00Z