Temperature dependence of protein motions in a thermophilic dihydrofolate reductase and its relationship to catalytic efficiency
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Plasticity of Cytochrome P450 2B4 as Investigated by Hydrogen-Deuterium Exchange Mass Spectrometry and X-ray CrystallographyPicosecond-resolved fluorescent probes at functionally distinct tryptophans within a thermophilic alcohol dehydrogenase: relationship of temperature-dependent changes in fluorescence to catalysis.An integrated model for enzyme catalysis emerges from studies of hydrogen tunneling.Hydrogen tunneling links protein dynamics to enzyme catalysisUpdate 1 of: Tunneling and dynamics in enzymatic hydride transfer.Multiple intermediates, diverse conformations, and cooperative conformational changes underlie the catalytic hydride transfer reaction of dihydrofolate reductase.Dynamic structural changes are observed upon collagen and metal ion binding to the integrin α1 I domain.The role of large-scale motions in catalysis by dihydrofolate reductase.Ligand-Dependent Conformational Dynamics of Dihydrofolate Reductase.Connecting protein conformational dynamics with catalytic function as illustrated in dihydrofolate reductase.Seeing the forest for the trees: fluorescence studies of single enzymes in the context of ensemble experiments.Two-dimensional infrared spectroscopy of azido-nicotinamide adenine dinucleotide in water.Comparative hydrogen-deuterium exchange for a mesophilic vs thermophilic dihydrofolate reductase at 25 °C: identification of a single active site region with enhanced flexibility in the mesophilic protein.Different dynamical effects in mesophilic and hyperthermophilic dihydrofolate reductases.Thermal adaptation of dihydrofolate reductase from the moderate thermophile Geobacillus stearothermophilus.Hydrogen-Deuterium Exchange of Lipoxygenase Uncovers a Relationship between Distal, Solvent Exposed Protein Motions and the Thermal Activation Barrier for Catalytic Proton-Coupled Electron Tunneling.Hydrogen-deuterium exchange reveals long-range dynamical allostery in soybean lipoxygenase.Enzymatic Kinetic Isotope Effects from Path-Integral Free Energy Perturbation Theory.Glutamine Hydrolysis by Imidazole Glycerol Phosphate Synthase Displays Temperature Dependent Allosteric Activation.Protein motions and dynamic effects in enzyme catalysis.
P2860
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P2860
Temperature dependence of protein motions in a thermophilic dihydrofolate reductase and its relationship to catalytic efficiency
description
2010 nî lūn-bûn
@nan
2010 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Temperature dependence of prot ...... onship to catalytic efficiency
@ast
Temperature dependence of prot ...... onship to catalytic efficiency
@en
type
label
Temperature dependence of prot ...... onship to catalytic efficiency
@ast
Temperature dependence of prot ...... onship to catalytic efficiency
@en
prefLabel
Temperature dependence of prot ...... onship to catalytic efficiency
@ast
Temperature dependence of prot ...... onship to catalytic efficiency
@en
P2093
P2860
P356
P1476
Temperature dependence of prot ...... onship to catalytic efficiency
@en
P2093
Judith P Klinman
Katheryn A Resing
Kevin M Sours
Natalie G Ahn
Olayinka A Oyeyemi
Thomas Lee
P2860
P304
10074-10079
P356
10.1073/PNAS.1003678107
P407
P577
2010-05-13T00:00:00Z