Mass Modulation of Protein Dynamics Associated with Barrier Crossing in Purine Nucleoside Phosphorylase.
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Fundamental challenges in mechanistic enzymology: progress toward understanding the rate enhancements of enzymesTriple Isotope Effects Support Concerted Hydride and Proton Transfer and Promoting Vibrations in Human Heart Lactate DehydrogenaseActive site and remote contributions to catalysis in methylthioadenosine nucleosidases.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 phosphorylaseAnother Look at the Mechanisms of Hydride Transfer Enzymes with Quantum and Classical Transition Path Sampling.Modulating Enzyme Catalysis through Mutations Designed to Alter Rapid Protein Dynamics.Hydride Transfer in DHFR by Transition Path Sampling, Kinetic Isotope Effects, and Heavy Enzyme StudiesThe Effect of Protein Mass Modulation on Human Dihydrofolate Reductase.Energy landscape of the Michaelis complex of lactate dehydrogenase: relationship to catalytic mechanism.Protein mass-modulated effects in the catalytic mechanism of dihydrofolate reductase: beyond promoting vibrations.Path Sampling Methods for Enzymatic Quantum Particle Transfer ReactionsConformational motions regulate phosphoryl transfer in related protein tyrosine phosphatases.Changes in protein architecture and subpicosecond protein dynamics impact the reaction catalyzed by lactate dehydrogenaseAre there dynamical effects in enzyme catalysis? Some thoughts concerning the enzymatic chemical step.Electric Fields and Fast Protein Dynamics in Enzymes.Catalytic-site design for inverse heavy-enzyme isotope effects in human purine nucleoside phosphorylase.Engineered control of enzyme structural dynamics and function.Promoting Vibrations and the Function of Enzymes. Emerging Theoretical and Experimental Convergence.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 dDirected Evolution as a Probe of Rate Promoting Vibrations Introduced via Mutational Change
P2860
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P2860
Mass Modulation of Protein Dynamics Associated with Barrier Crossing in Purine Nucleoside Phosphorylase.
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
2012年论文
@zh
2012年论文
@zh-cn
name
Mass Modulation of Protein Dyn ...... rine Nucleoside Phosphorylase.
@ast
Mass Modulation of Protein Dyn ...... rine Nucleoside Phosphorylase.
@en
type
label
Mass Modulation of Protein Dyn ...... rine Nucleoside Phosphorylase.
@ast
Mass Modulation of Protein Dyn ...... rine Nucleoside Phosphorylase.
@en
prefLabel
Mass Modulation of Protein Dyn ...... rine Nucleoside Phosphorylase.
@ast
Mass Modulation of Protein Dyn ...... rine Nucleoside Phosphorylase.
@en
P2093
P2860
P356
P1476
Mass Modulation of Protein Dyn ...... rine Nucleoside Phosphorylase.
@en
P2093
Dimitri Antoniou
Steven D Schwartz
Vern L Schramm
Xiaoxia Ge
P2860
P304
P356
10.1021/JZ301670S
P577
2012-12-01T00:00:00Z