Search results for "residue"

showing 10 items of 390 documents

Immunoassays for trifloxystrobin analysis. Part II. Assay development and application to residue determination in food.

2014

Immunochemical assays constitute complementary analytical methods for small organic molecule determination. We herein describe the characterisation and optimisation of two competitive enzyme-linked immunosorbent assays in different formats using monoclonal antibodies to the Quinone outside inhibitor (QoI) fungicide trifloxystrobin. Antibody selectivity was evaluated using a variety of agrochemicals and the main trifloxystrobin metabolite. Acceptable tolerance of the immunoassay to methanol, ethanol, and acetonitrile was observed in all cases, whereas a dissimilar influence of buffer pH and ionic strength was found. Moreover, the influence of Tween 20 over the analytical parameters was studi…

MetaboliteTrifloxystrobin metaboliteEnzyme-Linked Immunosorbent AssayAcetatesAnalytical ChemistryDeming regressionchemistry.chemical_compoundmedicineStrobilurinDetection limitImmunoassayResidue (complex analysis)ChromatographyPesticide residuesPesticide residuemedicine.diagnostic_testMolecular StructureChemistrycELISA formatGeneral MedicineStrobilurinsHaptenIonic strengthImmunoassayStrobilurinMethacrylatesIminesHaptenFood AnalysisFood ScienceFood chemistry
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Editorial: Antimicrobials in Wildlife and the Environment

2021

2 Pág. Centro de Investigación en Sanidad Animal (CISA)

Microbiology (medical)0303 health sciences030306 microbiologybusiness.industrywildlifeWildlifeAntimicrobialMicrobiologyQR1-502Biotechnology03 medical and health sciencesFood chainAntibiotic resistancefood chain[SDE]Environmental Sciencesantimicrobial residuesBusinessantimicrobial resistanceenvironmentComputingMilieux_MISCELLANEOUS030304 developmental biologyFrontiers in Microbiology
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Procedure for the Screening of Eggs and Egg Products to Detect Oxolonic Acid, Ciprofloxacin, Enrofloxacin, and Sarafloxacin Using Micellar Liquid Chr…

2019

A method based on micellar liquid chromatography was developed to determine oxolinic acid, ciprofloxacin, enrofloxacin, and sarafloxacin in eggs and egg products. The antimicrobial drugs were obtained in a micellar solution which was directly injected. The analytes were resolved using a C18 column and a mobile phase of 0.05 M sodium dodecyl sulfate—7.5% 1-propanol—0.5% triethylamine, buffered at pH 3 with phosphate salt, running under the isocratic mode. The signal was monitored by fluorescence. Validation was successfully performed according to the EU Commission Decision 2002/657/EC in terms of specificity, calibration range (LOQ to 1 mg/kg), linearity (R2 &gt

Microbiology (medical)Analytelaying hen01 natural sciencesBiochemistryMicrobiologyArticlechemistry.chemical_compoundSarafloxacinOxolinic acidEnrofloxacinmedicinePharmacology (medical)General Pharmacology Toxicology and PharmaceuticsTriethylamineDetection limitvalidationResidue (complex analysis)Chromatography010405 organic chemistryChemistry010401 analytical chemistrylcsh:RM1-950solid-to-liquid extraction0104 chemical sciencesfood safetyInfectious Diseaseslcsh:Therapeutics. PharmacologyMicellar liquid chromatographyfluorescenceoptimizationmedicine.drugAntibiotics
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Retrograde melt-residue interaction and the formation of near-anhydrous leucosomes in migmatites

2010

Considering physical segregation of melt from its residue, the chemical potentials of the components (oxides) are the same in both when segregation occurs. Then, as P–T conditions change, gradients in chemical potential are established between the melt-rich domains and residue permitting diffusional interaction to occur. In particular, on cooling, the chemical potential of H2O becomes higher in the melt segregation than in the residue, particularly when biotite becomes stable in the residue assemblage. Diffusion of water from the melt to the residue promotes crystallization of anhydrous products from the melt and hydrous products in the residue. This diffusive process, when coupled with mel…

MineralogyGeologyengineering.materialMigmatiteGranulitelaw.inventionResidue (chemistry)Chemical engineeringGeochemistry and PetrologylawengineeringAnhydrousPlagioclaseCrystallizationQuartzGeologyBiotiteJournal of Metamorphic Geology
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Conformational properties of N-acetyl-L-alanine N',N'-dimethylamide

2004

Ab initio/DFT analysis of the conformational properties of free Ac-Ala-NMe(2) (N-acetyl-L-alanine-N',N'-dimethylamide) in terms of the N-H.O, N-H.N, C-H.O hydrogen bonds and C(delta+) = O(delta-) dipole attractions was performed. The Ala residue combined with the C-terminal tertiary amide prefers an extended conformation and that characteristic of the (i + 1)th position of the betaVIb turn. These can be easily remodelled into a structure compatible with the (i + 1)th position of the betaII/betaVIa turn. The residue has also the potential to adopt the conformation accommodated at both central positions of the betaIII/betaIII' turn or the (i + 1)th position of the betaI/beta'I turn.

Models MolecularAlkylationProtein ConformationStereochemistryMolecular ConformationAb initioCalorimetryN-acetyl-L-alanineGeneral Biochemistry Genetics and Molecular Biologyab initio/DFT calculationschemistry.chemical_compoundResidue (chemistry)AmideN-alkylpeptidesPeptide designAlanineHydrogen bondN′N′-dimethylamidesAmidesβ-turnsDipoleCrystallographyAlanine derivativechemistryThermodynamicsPeptidesActa Biochimica Polonica
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Combined effect of the DeltaPhe or DeltaAla residue and the p-nitroanilide group on a didehydropeptides conformation.

2007

Two series of dehydropeptides of the general formulae Boc-Gly-X-Phe-p-NA, Boc-Gly-Gly-X-Phe-p-NA, Gly-X-Gly-Phe-p-NA·TFA, and Boc-Gly-X-Gly-Phe-p-NA, with X = ΔZPhe and ΔAla, were studied with NMR in DMSO and CDCl3-DMSO, and with CD in MeOH, MeCN, and TFE. The NMR spectra measured in DMSO suggest that peptides with the ΔPhe residue next to Phe are folded whereas peptides with Gly between ΔPhe and Phe are less ordered. NMR spectra of ΔAla-containing peptides indicate that these peptides are flexible and their conformational equilibria are populated by many different conformations. The CD spectra show that conformational properties of the peptides studied are distinctly influenced by a mutual…

Models MolecularCircular dichroismanimal structuresMagnetic Resonance SpectroscopyStereochemistryProtein ConformationPhenylalanineBiophysicsBiochemistryBiomaterialsResidue (chemistry)Spectroscopy Fourier Transform InfraredAlanineCrystallographyintegumentary systemChemistryMutual positionCircular DichroismOrganic ChemistryGeneral MedicineDipeptidesAmidesNMR spectra databaseSolventCrystallographyModels Chemicalembryonic structuresX-ray crystallographyBiopolymers
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Effect of the ΔPhe residue configuration on a didehydropeptides conformation: A combined CD and NMR study.

2010

Conformations of two pairs of dehydropeptides with the opposite configuration of the ΔPhe residue, Boc-Gly-Δ(Z)Phe-Gly-Phe-OMe (Z-OMe), Boc-Gly-Δ(E)Phe-Gly-Phe-OMe (E-OMe), Boc-Gly-Δ(Z)Phe-Gly-Phe-p-NA (Z-p-NA), and Boc-Gly-Δ(E)Phe-Gly-Phe-p-NA (E-p-NA) were compared on the basis of CD and NMR studies in MeOH, trifluoroethanol (TFE), MeCN, chloroform, and dimethylsulfoxide (DMSO). The CD results were used as the additional input data for the NMR-based determination of the detailed solution conformations of the peptides. It was found that E-OMe is unordered and Z-OMe, Z-p-NA, and E-p-NA adopt the β-turn conformation. There are two overlapping β-turns in each of those peptides: type II and ty…

Models MolecularCircular dichroismanimal structuresdehydropeptide conformationMagnetic Resonance SpectroscopyStereochemistryProtein ConformationPhenylalanineBiophysicsStereoisomerismBiochemistrydehydrophenylalanine configurationBiomaterialschemistry.chemical_compoundResidue (chemistry)Protein structureotorhinolaryngologic diseasesMoleculeAmino Acid SequencePeptide sequenceChloroformintegumentary systemMolecular StructureCircular DichroismOrganic ChemistryTemperatureStereoisomerismGeneral MedicineNuclear magnetic resonance spectroscopySolutionsnuclear magnetic resonancedehydropeptideschemistrySpectrophotometryOligopeptidesBiopolymers
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The unique structure of complete lipopolysaccharide isolated from semi-rough Plesiomonas shigelloides O37 (strain CNCTC 39/89) containing (2S)-O-(4-o…

2013

The complete structure of semi-rough lipopolysaccharide (SR-LPS) of Plesiomonas shigelloides CNCTC 39/89 (serotype O37) has been investigated by (1)H and (13)C NMR spectroscopy, matrix-assisted laser-desorption/ionization time-of-flight MS, and chemical methods. The following structure of the single unit of the O-antigen has been established: [formula see text] in which α-D-Lenp is (2S)-O-(4-oxopentanoic acid)-α-D-Glcp residue which has not been found in nature. The absolute configuration of oxopentanoic acid moiety in α-d-Lenose residue was determined by NOESY experiment combined with molecular modeling (MM2 force field). The decasaccharide core is substituted at C-4 of the β-D-Glcp residu…

Models MolecularMolecular modelStereochemistryMolecular Sequence DataAnalytical chemistryDisaccharideBiochemistryAnalytical Chemistrychemistry.chemical_compoundResidue (chemistry)GlucosidesCarbohydrate ConformationMoietybiologyOrganic ChemistryAbsolute configurationO AntigensGeneral MedicineCarbon-13 NMRbiology.organism_classificationLevulinic AcidsCarbohydrate SequencechemistryPlesiomonas shigelloidesPlesiomonasTwo-dimensional nuclear magnetic resonance spectroscopyCarbohydrate Research
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Crystal structures of bR(D85S) favor a model of bacteriorhodopsin as a hydroxyl-ion pump

2003

AbstractStructural features on the extracellular side of the D85S mutant of bacteriorhodopsin (bR) suggest that wild-type bR could be a hydroxyl-ion pump. A position between the protonated Schiff base and residue 85 serves as an anion-binding site in the mutant protein, and hydroxyl ions should have access to this site during the O-intermediate of the wild-type bR photocycle. The guanidinium group of R82 is proposed (1) to serve as a shuttle that eliminates the Born energy penalty for entry of an anion into this binding pocket, and conversely, (2) to block the exit of a proton or a related proton carrier.

Models MolecularProtein ConformationAnion Transport ProteinsBiophysicsBacteriorhodopsinProtonationCrystal structureCrystallography X-RayBiochemistryIon pumpIonchemistry.chemical_compoundResidue (chemistry)Structural BiologyMutant proteinHydroxidesGeneticsMolecular BiologyIon TransportSchiff basebiologyChemistryBacteriorhodopsinCell BiologyCrystallographyIon pumpBacteriorhodopsinsMutationbiology.proteinHydroxyl ionProtonsFEBS Letters
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Conformational investigation of alpha,beta-dehydropeptides. XIII. Conformational properties of N-acetyl-alpha,beta-dehydrovaline N',N'-dimethylamide.

2004

The crystal structure of Ac-DeltaVal-NMe(2) (DeltaVal = alpha,beta-dehydrovaline) was determined by X-ray crystallography. The found angles phi = -60 degrees and psi = 125 degrees correspond exactly to the respective values of the (i + 1)th residue in idealised beta-turn II/VIa. Ab initio/DFT studies revealed that the molecule adopts the angle psi restricted only to about |130 degrees | and very readily attains the angle phi = about -50 degrees. This is in line with its solid-state conformation. Taken together, these data suggest that the DeltaVal residue combined with a C-terminal tertiary amide is a good candidate at the (i + 1)th position in a type II/VIa beta-turn.

Models MolecularProtein ConformationStereochemistryMolecular ConformationAb initioAlpha (ethology)ValineCrystal structureCrystallography X-RayAmidesGeneral Biochemistry Genetics and Molecular BiologyCrystallographyResidue (chemistry)chemistry.chemical_compoundchemistryAmideX-ray crystallographyThermodynamicsMoleculeCrystallizationPeptidesBeta (finance)Acta Biochimica Polonica
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