Femtosecond dynamics coupled to chemical barrier crossing in a Born-Oppenheimer enzyme. - Wikidata - wikimedia - TriplyDB

Femtosecond dynamics coupled to chemical barrier crossing in a Born-Oppenheimer enzyme.

Femtosecond dynamics coupled to chemical barrier crossing in a Born-Oppenheimer enzyme.

http://www.wikidata.org/entity/Q35558827

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Fundamental challenges in mechanistic enzymology: progress toward understanding the rate enhancements of enzymes The role of protein dynamics in the evolution of new enzyme function Triple Isotope Effects Support Concerted Hydride and Proton Transfer and Promoting Vibrations in Human Heart Lactate Dehydrogenase Does 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 Reductase Active site and remote contributions to catalysis in methylthioadenosine nucleosidases.Rigidity, secondary structure, and the universality of the boson peak in proteins Coherent neutron scattering and collective dynamics in the protein, GFP.Hydrogen tunneling links protein dynamics to enzyme catalysis Evolution alters the enzymatic reaction coordinate of dihydrofolate reductase.Role of dynamics in enzyme catalysis: substantial versus semantic controversies.Isotope effects as probes for enzyme catalyzed hydrogen-transfer reactions.Transition States and transition state analogue interactions with enzymes.Isotope-specific and amino acid-specific heavy atom substitutions alter barrier crossing in human purine nucleoside phosphorylase Another Look at the Mechanisms of Hydride Transfer Enzymes with Quantum and Classical Transition Path Sampling.Mass Modulation of Protein Dynamics Associated with Barrier Crossing in Purine Nucleoside Phosphorylase.Heavy-enzyme kinetic isotope effects on proton transfer in alanine racemase.Modulating Enzyme Catalysis through Mutations Designed to Alter Rapid Protein Dynamics.Unraveling the role of protein dynamics in dihydrofolate reductase catalysis Kinetic isotope effects as a probe of hydrogen transfers to and from common enzymatic cofactors The power of integrating kinetic isotope effects into the formalism of the Michaelis-Menten equation.Transition States, analogues, and drug development.Relating localized protein motions to the reaction coordinate in coenzyme B₁₂-dependent enzymes.Protein dynamics and the enzymatic reaction coordinate.Linking protein motion to enzyme catalysis.Hydride Transfer in DHFR by Transition Path Sampling, Kinetic Isotope Effects, and Heavy Enzyme Studies The Effect of Protein Mass Modulation on Human Dihydrofolate Reductase.Energy landscape of the Michaelis complex of lactate dehydrogenase: relationship to catalytic mechanism.Dynamic and Electrostatic Effects on the Reaction Catalyzed by HIV-1 Protease.Different dynamical effects in mesophilic and hyperthermophilic dihydrofolate reductases.Protein mass-modulated effects in the catalytic mechanism of dihydrofolate reductase: beyond promoting vibrations.Path Sampling Methods for Enzymatic Quantum Particle Transfer Reactions Conformational motions regulate phosphoryl transfer in related protein tyrosine phosphatases.Changes in protein architecture and subpicosecond protein dynamics impact the reaction catalyzed by lactate dehydrogenase Excited state dynamics can be used to probe donor-acceptor distances for H-tunneling reactions catalyzed by flavoproteins.Pinpointing dynamic coupling in enzymes for efficient drug design.Increased dynamic effects in a catalytically compromised variant of Escherichia coli dihydrofolate reductase.Are there dynamical effects in enzyme catalysis? Some thoughts concerning the enzymatic chemical step.Structurally Linked Dynamics in Lactate Dehydrogenases of Evolutionarily Distinct Species.Role of Conformational Dynamics in the Evolution of Retro-Aldolase Activity.

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P2860

Femtosecond dynamics coupled to chemical barrier crossing in a Born-Oppenheimer enzyme.

http://www.wikidata.org/entity/Q35558827

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2011 nî lūn-bûn

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2011年の論文

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2011年論文

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2011年论文

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name

Femtosecond dynamics coupled to chemical barrier crossing in a Born-Oppenheimer enzyme.

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Femtosecond dynamics coupled to chemical barrier crossing in a Born-Oppenheimer enzyme.

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Femtosecond dynamics coupled to chemical barrier crossing in a Born-Oppenheimer enzyme.

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Femtosecond dynamics coupled to chemical barrier crossing in a Born-Oppenheimer enzyme.

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Femtosecond dynamics coupled to chemical barrier crossing in a Born-Oppenheimer enzyme.

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Femtosecond dynamics coupled to chemical barrier crossing in a Born-Oppenheimer enzyme.

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PNAS.1114900108

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Proceedings of the National Academy of Sciences of the United States of America

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Femtosecond dynamics coupled to chemical barrier crossing in a Born-Oppenheimer enzyme.

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Andrew S Murkin

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Rafael G Silva

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Vern L Schramm

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P2860

Neighboring Group Participation in the Transition State of Human Purine Nucleoside Phosphorylase †

Enzymatic transition states, transition-state analogs, dynamics, thermodynamics, and lifetimes

Transition state structure of 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase from Escherichia coli and its similarity to transition state analogues

At the dawn of the 21st century: Is dynamics the missing link for understanding enzyme catalysis?

The expression of isotope effects on enzyme-catalyzed reactions

A perspective on enzyme catalysis.

Atomic detail of chemical transformation at the transition state of an enzymatic reaction.

Enzyme millisecond conformational dynamics do not catalyze the chemical step.

Enzymatic transition states and dynamic motion in barrier crossing.

Cloning, overexpression, and purification of functional human purine nucleoside phosphorylase.

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