Two Dynamical Regimes of the Substrate Radical Rearrangement Reaction in B12-Dependent Ethanolamine Ammonia-Lyase Resolve Contributions of Native Protein Configurations and Collective Configurational Fluctuations to Catalysis.
about
Electron spin-labelling of the EutC subunit in B12-dependent ethanolamine ammonia-lyase reveals dynamics and a two-state conformational equilibrium in the N-terminal, signal-sequence-associated domain.Mesodomain and Protein-Associated Solvent Phases with Temperature-Tunable (200-265 K) Dynamics Surround Ethanolamine Ammonia-Lyase in Globally Polycrystalline Aqueous Solution Containing Dimethyl Sulfoxide.
P2860
Two Dynamical Regimes of the Substrate Radical Rearrangement Reaction in B12-Dependent Ethanolamine Ammonia-Lyase Resolve Contributions of Native Protein Configurations and Collective Configurational Fluctuations to Catalysis.
description
2017 nî lūn-bûn
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2017年の論文
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2017年学术文章
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2017年学术文章
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2017年學術文章
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name
Two Dynamical Regimes of the S ...... nal Fluctuations to Catalysis.
@en
Two Dynamical Regimes of the S ...... nal Fluctuations to Catalysis.
@nl
type
label
Two Dynamical Regimes of the S ...... nal Fluctuations to Catalysis.
@en
Two Dynamical Regimes of the S ...... nal Fluctuations to Catalysis.
@nl
prefLabel
Two Dynamical Regimes of the S ...... nal Fluctuations to Catalysis.
@en
Two Dynamical Regimes of the S ...... nal Fluctuations to Catalysis.
@nl
P2860
P1433
P1476
Two Dynamical Regimes of the S ...... nal Fluctuations to Catalysis.
@en
P2093
Meghan Kohne
P2860
P304
P356
10.1021/ACS.BIOCHEM.7B00294
P407
P50
P577
2017-06-15T00:00:00Z