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Conformational heterogeneity within the Michaelis complex of lactate dehydrogenase

Conformational heterogeneity within the Michaelis complex of lactate dehydrogenase

http://www.wikidata.org/entity/Q35036392

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Triple Isotope Effects Support Concerted Hydride and Proton Transfer and Promoting Vibrations in Human Heart Lactate Dehydrogenase Redox, haem and CO in enzymatic catalysis and regulation The dynamical nature of enzymatic catalysis.Direct evidence of catalytic heterogeneity in lactate dehydrogenase by temperature jump infrared spectroscopy Large scale dynamics of the Michaelis complex in Bacillus stearothermophilus lactate dehydrogenase revealed by a single-tryptophan mutant study Mechanism of Thermal Adaptation in the Lactate Dehydrogenases.Active-Loop Dynamics within the Michaelis Complex of Lactate Dehydrogenase from Bacillus stearothermophilus.Free energy surface of the Michaelis complex of lactate dehydrogenase: a network analysis of microsecond simulations Conformational Heterogeneity in the Michaelis Complex of Lactate Dehydrogenase: An Analysis of Vibrational Spectroscopy Using Markov and Hidden Markov Models Site-specific orientation of an α-helical peptide ovispirin-1 from isotope-labeled SFG spectroscopy Enzyme active site interactions by Raman/FTIR, NMR, and ab initio calculations Energy landscape of the Michaelis complex of lactate dehydrogenase: relationship to catalytic mechanism.Resolution of Submillisecond Kinetics of Multiple Reaction Pathways for Lactate Dehydrogenase.Mechanistic Analysis of Fluorescence Quenching of Reduced Nicotinamide Adenine Dinucleotide by Oxamate in Lactate Dehydrogenase Ternary Complexes.

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P2860

Conformational heterogeneity within the Michaelis complex of lactate dehydrogenase

http://www.wikidata.org/entity/Q35036392

description

2011 nî lūn-bûn

@nan

2011 թուականի Մայիսին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի մայիսին հրատարակված գիտական հոդված

@hy

2011年の論文

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2011年論文

@yue

2011年論文

@zh-hant

2011年論文

@zh-hk

2011年論文

@zh-mo

2011年論文

@zh-tw

2011年论文

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name

Conformational heterogeneity within the Michaelis complex of lactate dehydrogenase

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Conformational heterogeneity within the Michaelis complex of lactate dehydrogenase

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type

label

Conformational heterogeneity within the Michaelis complex of lactate dehydrogenase

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Conformational heterogeneity within the Michaelis complex of lactate dehydrogenase

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prefLabel

Conformational heterogeneity within the Michaelis complex of lactate dehydrogenase

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Conformational heterogeneity within the Michaelis complex of lactate dehydrogenase

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Journal of Physical Chemistry B

P1476

Conformational heterogeneity within the Michaelis complex of lactate dehydrogenase

@en

P2093

Hua Deng

http://www.w3.org/2001/XMLSchema#string

R Brian Dyer

http://www.w3.org/2001/XMLSchema#string

Robert Callender

http://www.w3.org/2001/XMLSchema#string

Ruel Desamero

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P2860

Protein dynamics and catalysis: the problems of transition state theory and the subtlety of dynamic control

Structure of a ternary complex of an allosteric lactate dehydrogenase from Bacillus stearothermophilus at 2.5 A resolution

Dynamics of folded proteins

The energy landscapes and motions of proteins

Fourier transform infrared techniques for probing membrane protein structure.

Nonresonance Raman difference spectroscopy: a general probe of protein structure, ligand binding, enzymatic catalysis, and the structures of other biomacromolecules.

Toward an understanding of the role of dynamics on enzymatic catalysis in lactate dehydrogenase.

Myoglobin: the hydrogen atom of biology and a paradigm of complexity

Structural transformations in the dynamics of Michaelis complex formation in lactate dehydrogenase

Advances in time-resolved approaches to characterize the dynamical nature of enzymatic catalysis.

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7670-7678

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scholarly article

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10.1021/JP2015929

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23

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2011-05-13T00:00:00Z

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