Search results for "structural biology"

showing 10 items of 827 documents

Purification of rat liver epoxide hydratase to apparent homogeneity.

1975

Epoxide hydratase (EC 4.2.1.63) is a microsomal enzyme which catalyses the conversion of epoxides to trans-dihydrodiols. Epoxides, produced by the action of microsomal monooxygenases (EC 1.14.1.1) from aromatic and olefinic compounds, are thought to be responsible for many of the harinful effects of polycyclic hydrocarbons and related compounds. Thus epoxide hydratase, together with glutathione 9transferases, (EC 2.5.1.18) may play an important role in the removal of carcinogenic and cytotoxic metabolites (for reviews see [l-3]). It has been reported [4,5] that dihydrodiols formed from some polycyclic hydrocarbons (benz(a)anthracene and benzo(a)pyrene) are reactivated by the microsomal mono…

chemistry.chemical_classificationEpoxide HydrolasesMaleAnthraceneBiophysicsCell BiologyGlutathioneMonooxygenaseBiochemistryRatsMolecular Weightchemistry.chemical_compoundEnzymechemistryBiochemistryStructural BiologyGeneticsMicrosomeMicrosomes LiverPyreneAnimalsPolycyclic HydrocarbonsMolecular BiologyCarcinogenHydro-LyasesFEBS letters
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Synthesis, infrared and M�ssbauer characterization and X-ray crystal structure of 1,10-phenanthrolinium tetrachloromethoxy phenylantimonate(V)

1991

The compound has been characterized by X-ray crystal structure determination, Mossbauer and i.r. spectroscopy. It crystallizes in the monoclinic space groupP21/c (No. 14) witha=24.228(4),b=8.335(2),c=23.975(4) A,β=117.83(3)° andZ=8. Least-squares refinement on 3749 observed reflections gave finalR=0.034 (Rw=0.037). The compound is constituted by [(C6H5)SbCl4OMe]− anions andphenH+cations. The coordination polyhedron about Sb is an octahedron (Sb-Cl 2.416(3), Sb-O 1.962(7) and Sb-C 2.138(9) A). The whole structure is characterized by two short contacts (O(1)⋯N(2) 2.76(1) O(2)⋯N(4) 2.75(1) A) involving the methoxy oxygens of the two independent anionic units [(C6H5)SbCl4OMe]− and two nitrogens…

chemistry.chemical_classificationGeneral ChemistryCrystal structureCondensed Matter Physicschemistry.chemical_compoundCrystallographychemistryOctahedronStructural BiologyX-ray crystallographyMössbauer spectroscopySpectroscopyInorganic compoundSpectroscopyOrganometallic chemistryMonoclinic crystal systemJournal of Crystallographic and Spectroscopic Research
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On the stability of the 24-meric hemocyanin from Eurypelma californicum.

1998

The stability of the 24-meric hemocyanin from Eurypelma californicum towards various denaturants (GdnHCl, urea, urea derivatives and salts of the Hofmeister series) indicates that the quaternary structure is stabilized by hydrophilic and polar forces. Thus, the interaction between the seven different subunit types of this cheliceratan hemocyanin is comparable with that of the closely related crustacean hemocyanins. In contrast, no significant influence of divalent ions such as Ca2+ and Mg2+ on the stability is observed at pH 8.0 and pH 8.5 but not at pH 7.0. Studies, both in the presence of urea and GdnHCl indicate that the denaturation process consists of a dissociation of the oligomeric s…

chemistry.chemical_classificationHofmeister seriesStereochemistryProtein subunitmedicine.medical_treatmentSpectrum AnalysisBiophysicsHemocyaninBiochemistryDissociation (chemistry)Divalentchemistry.chemical_compoundBiochemistrychemistryStructural BiologyHemocyaninsUreamedicineAnimalsProtein quaternary structureEurypelma californicumMolecular BiologyArthropodsBiochimica et biophysica acta
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Laccases: structure, reactions, distribution

2004

Laccases (EC 1.10.3.2, p-diphenol: dioxygen oxidoreductases) are multi-copper proteins that use molecular oxygen to oxidize various aromatic and non-aromatic compounds by a radical-catalyzed reaction mechanism. The enzymes are involved in the pathogenicity, immunity and morphogenesis of organisms and in the metabolic turnover of complex organic substances such as lignin or humic matter. Owing to their high non-specific oxidation capacity, laccases are useful biocatalysts for diverse biotechnological applications. Until recently, laccases were only found in eukaryotes (fungi, higher plants, insects), but now there is strong evidence for their widespread distribution in prokaryotes and the fi…

chemistry.chemical_classificationLaccaseProtein familyLaccaseGeneral Physics and AstronomyAscorbate OxidaseCell BiologyBiologyPathogenicityCatalysischemistry.chemical_compoundEnzymeBiochemistrychemistryStructural BiologyAnimalsLigninGeneral Materials ScienceMolecular oxygenBilirubin oxidaseCopperMicron
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Distribution of molecularly imprinted polymer layers on macroporous silica gel particles by STEM and EDX

2005

Abstract Using transmission electron microscopy (TEM) in parallel and scanning mode (STEM) combined with energy dispersive X-ray spectroscopy (EDX) the distribution of molecularly imprinted polymer layers covalently grafted on the inner and outer surface of macroporous silica gel particles was observed. The grafting was achieved using a special initiator system ( iniferter ) and applied on a well known model system producing molecularly imprinted layers with l -phenyl alanine analide ( l -PA) as template. By staining the sample with RuO 4 before its embedment in epoxy resin and cutting ultra thin slices it was possible to identify the stained grafted polymer on the silica matrix by EDX. Bas…

chemistry.chemical_classificationMaterials scienceSilica gelMolecularly imprinted polymerGeneral Physics and AstronomyCell BiologyPolymerEpoxychemistry.chemical_compoundchemistryChemical engineeringStructural BiologyTransmission electron microscopyCovalent bondvisual_artPolymer chemistryvisual_art.visual_art_mediumGeneral Materials ScienceSpectroscopyMolecular imprintingMicron
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The structure of gas-filled n-butyl-2-cyanoacrylate (BCA) polymer particles

1995

Abstract The structure of gas-filled poly-[n-butyl-2-cyanoacrylate] (BCA) particles has been demonstrated by negative staining with uranyl acetate, platinum-carbon shadowing of air-dried material and thin sectioning of the aqueous suspension of BCA particles, embedded in water-soluble melamine resin. The polymer shell of the hollow particles possesses a globular outer surface and a smoother inner surface.

chemistry.chemical_classificationMelamine resinMaterials scienceShell (structure)General Physics and AstronomyUranyl acetateCell BiologyPolymerengineering.materialAqueous suspensionNegative stainlaw.inventionPolymer particlechemistry.chemical_compoundChemical engineeringchemistryStructural BiologyCyanoacrylatelawPolymer chemistryengineeringGeneral Materials Scienceskin and connective tissue diseasesMicron
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Cooperative symmetric to asymmetric conformational transition of the apo-form of scavenger decapping enzyme revealed by simulations.

2007

Decapping is a central step in eukaryotic mRNA turnover and in gene expression regulation. The human scavenger decapping enzyme, DcpS, catalyses cap hydrolysis following mRNA degradation. DcpS is a dimeric enzyme, with two active sites. Crystal structures suggest that DcpS must undergo significant conformational changes upon ligand binding, but the mechanism of this transition is unknown. Here, we report two long timescale (20 ns) molecular dynamics simulations of the apo-form of DcpS. The dimer is observed to undergo a strikingly cooperative motion, with one active site closing while the other opens. The amplitude of the conformational change is 6–21 A and the apparent timescale is 4–13 ns…

chemistry.chemical_classificationMessenger RNAConformational changebiologyStereochemistryProtein ConformationDimerHydrolysisDCPSActive siteLigand (biochemistry)Crystallography X-RayBiochemistryCatalysisMolecular dynamicschemistry.chemical_compoundEnzymechemistryStructural BiologyEndoribonucleasesbiology.proteinHumansMolecular BiologyDimerizationProteins
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Photoaffinity cross-linking of F1ATPase from the thermophilic bacterium PS3 by 3′-arylazido-β-alanyl-2-azido ATP

1989

AbstractThe photoactivatable bifunctional 3′-arylazido-β-alanyl-2-azido ATP (2,3′-DiN3ATP) has been applied to study the localization of the nucleotide-binding sites of coupling factor 1 (F1ATPase, TF1) from the thermophilic bacterium PS3 by photoaffinity cross-linking. UV irradiation of TF1 in the presence of 2,3′-DiN3ATP results in the nucleotide-dependent formation of various higher molecular mass cross-links formed by two, three or even four α- and/or β-subunits. The differences observed upon photoaffinity cross-linking by the bifunctional 2-azido ATP or 8-azido ATP analog are discussed. They are probably due to the varied maximal distance between both azido groups, or to the different …

chemistry.chemical_classificationMolecular massbiologyStereochemistryProtein subunitNucleotide conformationBiophysicsCell Biologybiology.organism_classificationBiochemistrychemistry.chemical_compoundEnzymechemistryStructural BiologyGeneticsPhotoaffinity crosslinkingATPase F1-NucleotideNucleotide-binding siteBinding siteBifunctionalInterfacial localizationMolecular BiologyThermophilic bacterium PS3BacteriaFEBS Letters
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Moss cell cultures as sources of arachidonic and eicosapentaenoic acids

1986

AbstractLipid classes from tissue cultures of the moss Leptobryum pyriforme (Hedw.) Wils. were analyzed. In the total lipid fraction, this species contained 20% arachidonic acid and about 7% eicosapentaenoic acid. The distribution of these fatty acids showed a preference for the phospholipid fraction. In particular, the phosphatidylethanolamine fraction was enriched in arachidonic acid. The arachidonic acid content of Leptobryum could be altered by transferring the cultures to different culture conditions. Mosses show high organic mass production in tissue cultures in relatively simple media. The great potential of using mosses as sources for the production of polyunsaturated fatty acids is…

chemistry.chemical_classificationPhosphatidylethanolamineLeptobryum pyriformeGlycerideBiophysicsPhospholipidFatty acidCell BiologyBiologyFatty acidBiochemistryEicosapentaenoic acidPhospholipidTissue culturechemistry.chemical_compoundArachidonic acidchemistryBiochemistryStructural BiologyIcosapentaenoic acidGeneticsArachidonic acidCell cultureMolecular BiologyPolyunsaturated fatty acidFEBS Letters
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Photoaffinity labeling of the coupling factor 1 from the thermophilic bacterum PS3 by 8-azido ATP

1984

AbstractTo localize the nucleotide binding sites of the F1ATPase (TF1) from the thermophilic bacterium PS3 we have used 14C-labeled 8-azido ATP (8-N3ATP) as photoaffmity label. 8-N3ATP is hydrolyzed by the F,ATPase in the absence of ultraviolet light. Irradiation by ultraviolet light of the enzyme in the presence of 8-N3ATP results in reduction of ATPase activity and in preferential nucleotide specific labeling of the α subunits (0.8–0.9 mol 8-N3ATP/TF1,α:β = 4:1). Inactivation and labeling do not depend on the presence of Mg2+. Both effects decrease upon addition of various nucleotide di- or triphosphates.

chemistry.chemical_classificationPhotoaffinity labelingStereochemistryNoncatalytic nucleotide binding siteThermophileBiophysicsCell BiologyBiochemistryCoupling (electronics)HydrolysisEnzymechemistryStructural BiologyPhotoaffinity labelingMoleBacterial F1ATPaseGeneticsUltraviolet lightCatalytic nucleotide binding siteNucleotideThermophilic bacterium PS3Molecular BiologyFEBS Letters
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