Search results for "Escher"

showing 10 items of 728 documents

Membrane Structure of Aquaporin Observed with Combined Experimental and Theoretical Sum Frequency Generation Spectroscopy

2021

High-resolution structural information on membrane proteins is essential for understanding cell biology and for the structure-based design of new medical drugs and drug delivery strategies. X-ray diffraction (XRD) can provide angstrom-level information about the structure of membrane proteins, yet for XRD experiments, proteins are removed from their native membrane environment, chemically stabilized, and crystallized, all of which can compromise the conformation. Here, we describe how a combination of surface-sensitive vibrational spectroscopy and molecular dynamics simulations can account for the native membrane environment. We observe the structure of a glycerol facilitator channel (GlpF)…

GlycerolInfrared spectroscopyAquaporinPROTEINAquaporinsVIBRATIONAL SPECTROSCOPYMolecular dynamicsCHANNELElectrochemistryGeneral Materials SciencePEPTIDESpectroscopyCRYSTALChemistryEscherichia coli ProteinsSpectrum AnalysisMembrane structureWaterSurfaces and InterfacesCondensed Matter PhysicsBILAYERGLYCEROLINTERFACEMembraneMembrane proteinMOLECULAR-DYNAMICSBiophysicsMembrane channelORIENTATIONSum frequency generation spectroscopy
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The GlpF residue Trp219 is part of an amino-acid cluster crucial for aquaglyceroporin oligomerization and function

2018

The vestibule loop regions of aquaglyceroporins are involved in accumulation of glycerol inside the channel pore. Even though most loop regions do not show high sequence similarity among aquaglyceroporins, loop E is highly conserved in aquaglyceroporins, but not in members of the homologous aquaporins. Specifically, a tryptophan residue is extremely conserved within this loop. We have investigated the role of this residue (Trp219) that deeply protrudes into the protein and potentially interacts with adjacent loops, using the E. coli aqualgyeroporin GlpF as a model. Replacement of Trp219 affects the activity of GlpF and impairs the stability of the tetrameric protein. Furthermore, we have id…

GlycerolModels Molecular0301 basic medicineProtein ConformationTetrameric proteinBiophysicsAquaporinAquaporinsBiochemistry03 medical and health sciencesResidue (chemistry)TetramerEscherichia coliAmino Acidschemistry.chemical_classification030102 biochemistry & molecular biologyProtein StabilityChemistryEscherichia coli ProteinsTryptophanTryptophanCell BiologyAmino acid030104 developmental biologyAquaglyceroporinsBiochemistryMutationBiophysicsProtein foldingProtein MultimerizationAquaglyceroporinsBiochimica et Biophysica Acta (BBA) - Biomembranes
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Microbial and chemical origins of the bactericidal activity of thermally treated yellow mustard powder toward Escherichia coli O157:H7 during dry sau…

2010

Abstract Work examines the origin of bactericidal activity in mustard flour and explores the relative contribution from starter cultures, E. coli O157:H7 itself and other sources. Bacteria can degrade naturally occurring glucosinolates in mustard and form isothiocyanates with antimicrobial activity. In the present work, 24 starter cultures (mostly from commercial mixtures) were screened for their capacity to decompose the glucosinolate, sinalbin. The most active pair, Pediococcus pentosaceus UM 121P and Staphylococcus carnosus UM 123M, were used together for the production of dry fermented sausage contaminated with E. coli O157:H7 (~ 6.5 log CFU/g). They were compared to industrial starters…

Glycoside HydrolasesStaphylococcusColony Count MicrobialFood ContaminationEscherichia coli O157medicine.disease_causeMicrobiologyCholineMicrobiologychemistry.chemical_compoundStarterIsothiocyanatesmedicinePediococcusFood scienceEscherichia coliStaphylococcus carnosusbiologyMyrosinasefood and beveragesGeneral MedicineAntimicrobialbiology.organism_classificationAnti-Bacterial AgentsSinalbinMeat ProductschemistryGlucosinolateFermentationFood MicrobiologyFermentationPowdersMustard PlantFood ScienceInternational Journal of Food Microbiology
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Probing suggested catalytic domains of glycosyltransferases by site-directed mutagenesis.

2003

The plant enzyme arbutin synthase isolated from cell suspension cultures of Rauvolfia serpentina and heterologously expressed in Escherichia coli is a member of the NRD1beta family of glycosyltransferases. This enzyme was used to prove, by site-directed mutagenesis, suggested catalytic domains and reaction mechanisms proposed for enzyme-catalyzed glycosylation. Replacement of amino acids far from the NRD domain do not significantly affect arbutin synthase activity. Exchange of amino acids at the NRD site leads to a decrease of enzymatic activity, e.g. substitution of Glu368 by Asp. Glu368, which is a conserved amino acid in glycosyltransferases located at position 2 and is important for enz…

GlycosylationStereochemistryMolecular Sequence DataBiologyBiochemistryPolymerase Chain ReactionGene Expression Regulation EnzymologicRauwolfiaSubstrate Specificitychemistry.chemical_compoundCatalytic DomainGlycosyltransferaseEscherichia coliAmino Acid SequenceSite-directed mutagenesisConserved SequenceDNA Primerschemistry.chemical_classificationBinding SitesATP synthaseSequence Homology Amino AcidMutagenesisArbutinGlycosyltransferasesEnzyme assayRecombinant ProteinsAmino acidEnzymechemistryBiochemistryAmino Acid Substitutionbiology.proteinMutagenesis Site-DirectedEuropean journal of biochemistry
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Phospholipid distribution in the cytoplasmic membrane of Gram-negative bacteria is highly asymmetric, dynamic, and cell shape-dependent

2020

The cell shape of Gram-negative bacteria is maintained metabolically by asymmetric lipid distribution in biogenic plasma membrane.

Gram-negative bacteriaPhospholipidBiochemistryMicrobiology03 medical and health scienceschemistry.chemical_compoundGram-Negative BacteriaCardiolipinEscherichia coliInner membraneCell ShapePhospholipidsResearch Articles030304 developmental biologyPhosphatidylethanolamine0303 health sciencesMultidisciplinarybiologyBilayer030302 biochemistry & molecular biologyCell MembraneSciAdv r-articlesPeriplasmic spacebiology.organism_classificationchemistryCytoplasmBiophysicslipids (amino acids peptides and proteins)Research Article
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Isolation of carcinoembryonic antigen N-terminal domains (N-A1) from soluble aggregates

2011

Abstract Carcinoembryonic antigen (CEA) was identified as a prominent tumor-associated antigen in human colorectal cancer and it is still intensively investigated. However, its physiological role remains unclear. The CEA molecule is composed of seven highly hydrophobic, immunoglobulin-like domains, six of which contain a single disulphide bridge. The production of recombinant protein containing Ig-like domains in bacterial expression systems often results in partial degradation or insolubility due to aggregation hampering the analysis of their native structure and function. Here, we present a new method of expression and purification of CEA N-terminal domains (N-A1) fused to MBP in Escheric…

Guanidinium chlorideCircular dichroismRecombinant Fusion Proteinsmedicine.disease_causeMaltose-Binding Proteinslaw.inventionchemistry.chemical_compoundCarcinoembryonic antigenlawProtein purificationEscherichia colimedicineTEV proteaseHumansDisulfidesEscherichia coliGuanidinebiologyProtein StabilityCircular DichroismFusion proteinCarcinoembryonic AntigenProtein Structure TertiarySolubilitychemistryBiochemistryChromatography GelRecombinant DNAbiology.proteinElectrophoresis Polyacrylamide GelBiotechnologyProtein Expression and Purification
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Oxidative DNA base damage induced by singlet oxygen and photosensitization: recognition by repair endonucleases and mutagenicity.

2000

We have analyzed the recognition by various repair endonucleases of DNA base modifications induced by three oxidants, viz. [4-(tert-butyldioxycarbonyl)benzyl]triethylammonium chloride (BCBT), a photochemical source of tert-butoxyl radicals, disodium salt of 1,4-etheno-2,3-benzodioxin-1,4-dipropanoic acid (NDPO(2)), a chemical source of singlet oxygen, and riboflavin, a type-I photosensitizer. The base modifications induced by BCBT, which were previously shown to be mostly 7,8-dihydro-8-oxoguanine (8-oxoGua) residues, were recognized by Fpg and Ogg1 proteins, but not by endonuclease IIII, Ntg1 and Ntg2 proteins. In the case of singlet oxygen induced damage, 8-oxoGua accounted for only 35% of…

GuanineDNA LigasesLightGuanineDNA damageRiboflavinMolecular Sequence DataToxicologySubstrate Specificitychemistry.chemical_compoundEndonucleaseBacterial ProteinsGeneticsPhotosensitizerPentosyltransferasesMolecular BiologybiologyBase SequenceSinglet oxygenEscherichia coli ProteinsMutagenesisCorticoviridaeProteinsEndonucleasesDNA-(apurinic or apyrimidinic site) lyaseOxygenBiochemistrychemistryDNA ViralMutationbiology.proteinOxidation-ReductionDNADNA DamageMutation research
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tert-Butoxyl radicals generate mainly 7,8-dihydro-8-oxoguanine in DNA.

2000

Abstract Like hydroxyl radicals, alkoxyl radicals have been implicated in the generation of cellular oxidative DNA damage under physiological conditions; however, their genotoxic potential has not yet been established. We have analyzed the DNA damage induced by a photochemical source of tert- butoxyl radicals, the water soluble peroxy ester [4-( tert -butyldioxycarbonyl)benzyl]triethylammonium chloride (BCBT), using various repair endonucleases as probes. The irradiation (UV 360 ) of BCBT in the presence of bacteriophage PM2 DNA was found to generate a DNA damage profile that consisted mostly of base modifications sensitive to the repair endonuclease Fpg protein. Approximately 90% of the mo…

GuaninePyrimidineDNA damageStereochemistryUltraviolet RaysRadicalMolecular Sequence DataBiologyToxicologymedicine.disease_causechemistry.chemical_compoundBacterial ProteinsGeneticsmedicinePentosyltransferasesMolecular BiologyBase SequencePoint mutationEscherichia coli ProteinsMutagenesisCorticoviridaeProteins8-OxoguanineQuaternary Ammonium CompoundsBiochemistrychemistryMutagenesisAlcoholsDNA ViralOxidative stressDNADNA DamagePlasmidsMutation research
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Zur Pathologie und Klinik der h�morrhagischen und nekrotisierenden S�uglingsenteritis durch Escherichia coli O 127?B 8

1961

Klinischer Verlauf und pathologisch-anatomische Befunde von 25 Sauglingen im 1. Trimenon, die im Verlauf einer Enteritisepidemie durch Escherichia coli O 127: B 8 verstorben waren, werden ausfuhrlich dargestellt. Es werden epidemiologische Fragen erortert und klinisch ein perakuter Krankheitsverlauf bei Fruhgeborenen und eine protrahierte Form bei alteren Kindern unterschieden. Morphologisch bestand eine ungewohnlich schwere bamorrhagische und nekrotisierende Enteritis mit Geschwurbildung. Die Enteritis hatte bei den Sauglingen der jungeren Altersgruppe den gesamten Verdauungskanal von Oesophagus bis Rectum befallen, bei alteren Kindern blieb die Enteritis auf Dunndarm und Colonteile beschr…

Gynecologymedicine.medical_specialtybusiness.industryPediatrics Perinatology and Child HealthMedicinebusinessmedicine.disease_causemedicine.diseaseEscherichia coliEnteritisZeitschrift f�r Kinderheilkunde
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Detection of oxidative mutagenesis by isoniazid and other hydrazine derivatives in Escherichia coli WP2 tester strain IC203, deficient in OxyR: stron…

1998

Abstract Strain IC203, deficient in the OxyR function, was sensitive to both cytotoxic and mutagenic effects of isoniazid (INH) whereas its parent, WP2 uvrA /pKM101, was resistant to these effects. Four other hydrazine compounds, hydrazine hydrate (HZH), phenylhydrazine (PHZ), hydralazine (HLZ) and nialamide (NLD), were mutagenic in WP2 uvrA /pKM101. Increases in mutagenicity were observed in IC203 for HZH and PHZ but not for HLZ and NLD. Growth inhibition zones by HZH, PHZ and NLD were larger in IC203 than in WP2 uvrA /pKM101. The enhancements in the effects of INH, HZH and PHZ in IC203 with respect to its oxyR + parent are considered to be caused by the production of reactive oxygen speci…

Health Toxicology and Mutagenesismedicine.disease_causechemistry.chemical_compoundSpecies SpecificityEscherichia coliIsoniazidGeneticsmedicineAnimalsEscherichia coliPhenylhydrazinechemistry.chemical_classificationReactive oxygen speciesbiologyMutagenicity TestsEscherichia coli ProteinsMutagenesisbiology.organism_classificationEnterobacteriaceaeRatsDNA-Binding ProteinsRepressor ProteinsLiverBiochemistrychemistryMutagenesisCatalasebiology.proteinbacteriaGrowth inhibitionReactive Oxygen SpeciesOxidation-ReductionCytosineMutagensTranscription FactorsMutation Research/Genetic Toxicology and Environmental Mutagenesis
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