The rates of defined changes in protein structure during the catalytic cycle of lactate dehydrogenase.
about
Dynamic dissociating homo-oligomers and the control of protein functionLactate dehydrogenase undergoes a substantial structural change to bind its substrateThe dynamical nature of enzymatic catalysis.Site-directed mutagenesis reveals role of mobile arginine residue in lactate dehydrogenase catalysis.The approach to the Michaelis complex in lactate dehydrogenase: the substrate binding pathwayDirect evidence of catalytic heterogeneity in lactate dehydrogenase by temperature jump infrared spectroscopyLarge scale dynamics of the Michaelis complex in Bacillus stearothermophilus lactate dehydrogenase revealed by a single-tryptophan mutant studyMechanism of Thermal Adaptation in the Lactate Dehydrogenases.Active-Loop Dynamics within the Michaelis Complex of Lactate Dehydrogenase from Bacillus stearothermophilus.On the pathway of forming enzymatically productive ligand-protein complexes in lactate dehydrogenase.An insecticidal GroEL protein with chitin binding activity from Xenorhabdus nematophilaThermal activation of 'allosteric-like' large-scale motions in a eukaryotic Lactate Dehydrogenase.Kinetic differentiation between enzyme inactivation involving complex-formation with the inactivator and that involving a conformation-change step.Catalytic-rate improvement of a thermostable malate dehydrogenase by a subtle alteration in cofactor binding.Activity of heart and muscle lactate dehydrogenases in all-aqueous systems and in organic solvents with low amounts of water. Effect of guanidine chloride.Activity-Related Microsecond Dynamics Revealed by Temperature-Jump Förster Resonance Energy Transfer Measurements on Thermophilic Alcohol Dehydrogenase.Thermodynamic and Structural Adaptation Differences between the Mesophilic and Psychrophilic Lactate Dehydrogenases.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.Activity and fluorescence changes of lactate dehydrogenase induced by guanidine hydrochloride in reverse micelles.
P2860
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P2860
The rates of defined changes in protein structure during the catalytic cycle of lactate dehydrogenase.
description
1985 nî lūn-bûn
@nan
1985 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1985 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
1985年の論文
@ja
1985年論文
@yue
1985年論文
@zh-hant
1985年論文
@zh-hk
1985年論文
@zh-mo
1985年論文
@zh-tw
1985年论文
@wuu
name
The rates of defined changes i ...... ycle of lactate dehydrogenase.
@ast
The rates of defined changes i ...... ycle of lactate dehydrogenase.
@en
type
label
The rates of defined changes i ...... ycle of lactate dehydrogenase.
@ast
The rates of defined changes i ...... ycle of lactate dehydrogenase.
@en
prefLabel
The rates of defined changes i ...... ycle of lactate dehydrogenase.
@ast
The rates of defined changes i ...... ycle of lactate dehydrogenase.
@en
P2093
P1476
The rates of defined changes i ...... ycle of lactate dehydrogenase.
@en
P2093
A D Waldman
A R Clarke
J J Holbrook
P304
P356
10.1016/0167-4838(85)90250-X
P407
P577
1985-07-01T00:00:00Z