about
The structure of ActVA-Orf6, a novel type of monooxygenase involved in actinorhodin biosynthesis.The B(12)-binding subunit of glutamate mutase from Clostridium tetanomorphum traps the nucleotide moiety of coenzyme B(12)Structural basis for the enhanced stability of highly fluorinated proteinsStructures of benzylsuccinate synthase elucidate roles of accessory subunits in glycyl radical enzyme activation and activityProtein-coenzyme interactions in adenosylcobalamin-dependent glutamate mutaseAldehyde Decarbonylases: Enigmatic Enzymes of Hydrocarbon BiosynthesisUsing fluorous amino acids to probe the effects of changing hydrophobicity on the physical and biological properties of the beta-hairpin antimicrobial peptide protegrin-1.Cation-pi interactions studied in a model coiled-coil peptideModulating protein structure with fluorous amino acids: increased stability and native-like structure conferred on a 4-helix bundle protein by hexafluoroleucine.Fluorinated proteins: from design and synthesis to structure and stability.Design, synthesis, and study of fluorinated proteins.Engineered Surface-Immobilized Enzyme that Retains High Levels of Catalytic Activity in Air.Insights into substrate and metal binding from the crystal structure of cyanobacterial aldehyde deformylating oxygenase with substrate bound.Hydrogen tunneling in adenosylcobalamin-dependent glutamate mutase: evidence from intrinsic kinetic isotope effects measured by intramolecular competition.Solvent isotope effects on alkane formation by cyanobacterial aldehyde deformylating oxygenase and their mechanistic implicationsRecent advances in radical SAM enzymology: new structures and mechanisms.Adenosyl radical: reagent and catalyst in enzyme reactions.High-resolution NMR characterization of low abundance oligomers of amyloid-β without purificationSubstrate-bound structures of benzylsuccinate synthase reveal how toluene is activated in anaerobic hydrocarbon degradation.Reaction of adenosylcobalamin-dependent glutamate mutase with 2-thiolglutarate.Deuterium isotope effects in the unusual addition of toluene to fumarate catalyzed by benzylsuccinate synthase.Insights into the mechanisms of adenosylcobalamin (coenzyme B12)-dependent enzymes from rapid chemical quench experiments.Fluorine--a new element in the design of membrane-active peptides.Mechanistic insights from reaction of α-oxiranyl-aldehydes with cyanobacterial aldehyde deformylating oxygenase.Using (19)F NMR to probe biological interactions of proteins and peptides.Perfluoro-tert-butyl-homoserine as a sensitive 19F NMR reporter for peptide-membrane interactions in solution.Mechanism of benzylsuccinate synthase probed by substrate and isotope exchange.Role of active site residues in promoting cobalt-carbon bond homolysis in adenosylcobalamin-dependent mutases revealed through experiment and computation.Isofunctional enzymes PAD1 and UbiX catalyze formation of a novel cofactor required by ferulic acid decarboxylase and 4-hydroxy-3-polyprenylbenzoic acid decarboxylase.Cloning and sequencing of glutamate mutase component E from Clostridium tetanomorphum. Organization of the mut genes.Role of zinc in human islet amyloid polypeptide aggregation.Using fluorine nuclear magnetic resonance to probe the interaction of membrane-active peptides with the lipid bilayer.Conversion of (3S,4R)-tetrahydrodaidzein to (3S)-equol by THD reductase: proposed mechanism involving a radical intermediate.The role of the active site glutamate in the rearrangement of glutamate to 3-methylaspartate catalyzed by adenosylcobalamin-dependent glutamate mutase.Photolysis and recombination of adenosylcobalamin bound to glutamate mutase.Pre-steady-state measurement of intrinsic secondary tritium isotope effects associated with the homolysis of adenosylcobalamin and the formation of 5'-deoxyadensosine in glutamate mutase.Role of Arg100 in the active site of adenosylcobalamin-dependent glutamate mutase.Using fluorine nuclear magnetic resonance to probe changes in the structure and dynamics of membrane-active peptides interacting with lipid bilayers.Isotope effects for deuterium transfer between substrate and coenzyme in adenosylcobalamin-dependent glutamate mutase.Molecular orientation of enzymes attached to surfaces through defined chemical linkages at the solid-liquid interface.
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P50
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forsker
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onderzoeker
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researcher ORCID ID = 0000-0003-1713-1683
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name
E. Neil G. Marsh
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E. Neil G. Marsh
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Neil Marsh
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Neil Marsh
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E. Neil G. Marsh
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E. Neil G. Marsh
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Neil Marsh
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Neil Marsh
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E. Neil G. Marsh
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E. Neil G. Marsh
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E. Neil G. Marsh
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Neil Marsh
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Neil Marsh
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P106
P31
P496
0000-0003-1713-1683