1999
Crystallographic Studies of Phosphonate-Based α-Reaction Transition-State Analogues Complexed to Tryptophan Synthase † , ‡
Sachpatzidis A, Dealwis C, Lubetsky J, Liang P, Anderson K, Lolis E. Crystallographic Studies of Phosphonate-Based α-Reaction Transition-State Analogues Complexed to Tryptophan Synthase † , ‡. Biochemistry 1999, 38: 12665-12674. PMID: 10504236, DOI: 10.1021/bi9907734.Peer-Reviewed Original ResearchMeSH KeywordsCrystallography, X-RayEnzyme InhibitorsHydrogen BondingModels, MolecularOrganophosphonatesTryptophan SynthaseConceptsTransition stateShort hydrogen bondsTryptophan synthaseHigh conformational flexibilityTetrahedral transition stateTransition state analogueMechanism of catalysisEnzyme-inhibitor complexStructure-based approachPhosphonate oxygenIndole-3-glycerol phosphateHydroxyl oxygenHydrogen bondsSulfur atomsActive siteC3 atomC2 atomCrystal structureConformational flexibilityCrystallographic studiesInhibitor bindingConformation changeAtomsNew herbicidesGlu-49
1998
Macrophage Migration Inhibitory Factor Interactions with Glutathione and S -Hexylglutathione*
Swope M, Sun H, Klockow B, Blake P, Lolis E. Macrophage Migration Inhibitory Factor Interactions with Glutathione and S -Hexylglutathione*. Journal Of Biological Chemistry 1998, 273: 14877-14884. PMID: 9614090, DOI: 10.1074/jbc.273.24.14877.Peer-Reviewed Original ResearchBinding SitesCircular DichroismEnzyme InhibitorsFluorescenceGlutathioneHumansHydrogen-Ion ConcentrationIntramolecular OxidoreductasesMacrophage Migration-Inhibitory FactorsMagnetic Resonance SpectroscopyModels, MolecularProtein BindingProtein ConformationProtein FoldingRecombinant ProteinsSulfhydryl Compounds