Search results for "Nuclear Magnetic Resonance Spectroscopy"

showing 10 items of 843 documents

The New Structure of Core Oligosaccharide Presented by Proteus penneri 40A and 41 Lipopolysaccharides

2018

The new type of core oligosaccharide in Proteus penneri 40A and 41 lipopolysaccharides has been investigated by 1H and 13C NMR spectroscopy, electrospray ionization mass spectrometry and chemical methods. Core oligosaccharides of both strains were chosen for structural analysis based on the reactivity of LPSs with serum against P. penneri 40A core oligosaccharide–diphtheria toxoid conjugate. Structural analyses revealed that P. penneri 40A and 41 LPSs possess an identical core oligosaccharide.

0301 basic medicineLipopolysaccharidesSpectrometry Mass Electrospray IonizationMagnetic Resonance SpectroscopyStereochemistryElectrospray ionizationOligosaccharidesanti-conjugate serum; core oligosaccharide; lipopolysaccharide; NMR spectroscopy; ESI MS; <i>Proteus penneri</i>Immune seraProteus penneriCatalysisArticleInorganic Chemistrycore oligosaccharidelcsh:Chemistry03 medical and health sciencesStructure-Activity Relationship13c nmr spectroscopyNMR spectroscopyMoleculePhysical and Theoretical ChemistryESI MSMolecular Biologylcsh:QH301-705.5SpectroscopyAntigens Bacterial030102 biochemistry & molecular biologybiologyMolecular StructureChemistryCore oligosaccharideImmune Seraanti-conjugate serumOrganic ChemistrylipopolysaccharideGeneral MedicineNuclear magnetic resonance spectroscopybiology.organism_classificationProteus penneriComputer Science Applicationslcsh:Biology (General)lcsh:QD1-999ConjugateInternational Journal of Molecular Sciences
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Oleanane-type glycosides from the roots of Weigela florida “rumba” and evaluation of their antibody recognition

2018

Three triterpene glycosides were isolated from the roots of Weigela florida "rumba" (Bunge) A. DC.: two previously undescribed 3-O-β-d-xylopyranosyl-(1→2)-[β-d-xylopyranosyl-(1→4)]-β-d-xylopyranosyl-(1→4)-β-d-xylopyranosyl-(1→3)-α-L-rhamnopyranosyl-(1→2)-α-l-arabinopyranosyloleanolic acid (1) and 3-O-β-d-xylopyranosyl-(1→2)-[β-d-glucopyranosyl-(1→4)]-β-d-xylopyranosyl-(1→4)-β-d-xylopyranosyl-(1→3)-α-l-rhamnopyranosyl-(1→2)-α-L-arabinopyranosyloleanolic acid (2), and one isolated for the first time from a natural source 3-O-β-d-xylopyranosyl-(1→3)-α-l-rhamnopyranosyl-(1→2)-α-l-arabinopyranosyloleanolic acid (3). Their structures were elucidated mainly by 2D NMR spectroscopic analysis (COSY, …

0301 basic medicineMultiple SclerosisStereochemistryEnzyme-Linked Immunosorbent AssayCaprifoliaceaePlant Roots01 natural sciences03 medical and health scienceschemistry.chemical_compoundTriterpeneDrug DiscoveryHumansGlycosidesOleanolic AcidCaprifoliaceaeOleanolic acidOleananePharmacologychemistry.chemical_classificationMolecular Structurebiology010405 organic chemistryGlycosideGeneral Medicinebiology.organism_classification0104 chemical sciences030104 developmental biologyImmunoglobulin MchemistryImmunoglobulin Mbiology.proteinAntibodyTwo-dimensional nuclear magnetic resonance spectroscopyFitoterapia
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Lunasin is a redox sensitive intrinsically disordered peptide with two transiently populated α-helical regions.

2016

Lunasin is a 43 amino acid peptide with anti-cancer, antioxidant, anti-inflammatory and cholesterol-lowering properties. Although the mechanism of action of lunasin has been characterized to some extent, its exact three-dimensional structure as well as the function of the N-terminal sequence remains unknown. We established a novel method for the production of recombinant lunasin that allows efficient isotope labeling for NMR studies. Initial studies showed that lunasin can exist in a reduced or oxidized state with an intramolecular disulfide bond depending on solution conditions. The structure of both forms of the peptide at pH 3.5 and 6.5 was characterized by CD spectroscopy and multidimen…

0301 basic medicineProtein Conformation alpha-HelicalCircular dichroismPhysiologyBeta sheetPeptideIntrinsically disordered proteinsBiochemistryLunasinAntioxidantsHistones03 medical and health sciencesCellular and Molecular Neuroscience0302 clinical medicineEndocrinologyNeoplasmsAnticarcinogenic AgentsHumansAmino Acid SequenceDisulfidesProtein secondary structureNuclear Magnetic Resonance BiomolecularPlant Proteinschemistry.chemical_classificationChemistryAcetylationNuclear magnetic resonance spectroscopyIntrinsically Disordered Proteins030104 developmental biologyBiochemistry030220 oncology & carcinogenesisBiophysicsSoybean ProteinsPeptidesOxidation-ReductionFunction (biology)Peptides
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Zero-field nuclear magnetic resonance of chemically exchanging systems.

2019

Zero- to ultralow-field (ZULF) nuclear magnetic resonance (NMR) is an emerging tool for precision chemical analysis. In this work, we study dynamic processes and investigate the influence of chemical exchange on ZULF NMR J-spectra. We develop a computational approach that allows quantitative calculation of J-spectra in the presence of chemical exchange and apply it to study aqueous solutions of [15N]ammonium (15N\documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}$${\mathrm{H}}_4^ +$$\end{document}H4+) as a model syst…

0301 basic medicineReaction kinetics and dynamicsSciencePhysics::Medical PhysicsGeneral Physics and AstronomyModel system02 engineering and technologyGeneral Biochemistry Genetics and Molecular BiologyArticle03 medical and health sciencesNuclear magnetic resonanceZero fieldHyperpolarization (physics)lcsh:ScienceDissolutionQuantitative Biology::Biomolecules3403 Macromolecular and Materials ChemistryMultidisciplinaryAqueous solution34 Chemical SciencesChemical exchangeQ500Diagnostic markersGeneral ChemistryNuclear magnetic resonance spectroscopy021001 nanoscience & nanotechnologyequipment and supplies030104 developmental biologylcsh:Qddc:5000210 nano-technologyhuman activitiesSolution-state NMR51 Physical Sciences
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Monitoring few molecular binding events in scalable confined aqueous compartments by raster image correlation spectroscopy (CADRICS)

2016

The assembly of scalable liquid compartments for binding assays in array formats constitutes a topic of fundamental importance in life sciences. This challenge can be addressed by mimicking the structure of cellular compartments with biological native conditions. Here, inkjet printing is employed to develop up to hundreds of picoliter aqueous droplet arrays stabilized by oil-confinement with mild surfactants (Tween-20). The aqueous environments constitute specialized compartments in which biomolecules may exploit their function and a wide range of molecular interactions can be quantitatively investigated. Raster Image Correlation Spectroscopy (RICS) is employed to monitor in each compartmen…

0301 basic medicineStreptavidinBiomedical EngineeringMolecular bindingBiotinBioengineeringNanotechnology02 engineering and technologydroplets microarrays inkjet printing Raster Image Correlation Spectroscopy water-in-oil emulsion StreptvidinBiochemistry03 medical and health scienceschemistry.chemical_compoundCompartment (pharmacokinetics)Cellular compartmentchemistry.chemical_classificationAqueous solutionSpectrum AnalysisBiomoleculeWaterGeneral Chemistrycomputer.file_formatMicroarray Analysis021001 nanoscience & nanotechnology030104 developmental biologychemistryPrintingInkStreptavidinRaster graphics0210 nano-technologycomputerTwo-dimensional nuclear magnetic resonance spectroscopyLab on a Chip
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Age and muscle function are more closely associated with intracellular magnesium, as assessed by 31P magnetic resonance spectroscopy, than with serum…

2019

Total serum magnesium is a common clinical measurement for assessing magnesium status; however, magnesium in blood represents less than 1% of the body’s total magnesium content. We measured intramuscular ionized magnesium by phosphorus magnetic resonance spectroscopy (31P-MRS) and tested the hypothesis that this measure better correlates with skeletal muscle function and captures more closely the effect of aging than the traditional measure of total serum magnesium. Data were collected from 441 participants (age 24–98 years) in the Baltimore Longitudinal Study of Aging (BLSA), a study of normative aging that encompasses a broad age range. Results showed that intramuscular ionized magnesium …

0301 basic medicinemedicine.medical_specialtySettore MED/09 - Medicina InternaPhysiologychemistry.chemical_element030209 endocrinology & metabolismmagnesiumIonized magnesiumlcsh:Physiologysarcopenia03 medical and health sciences0302 clinical medicineNegatively associatedPhysiology (medical)Internal medicineMedicineskeletal muscle31P magnetic resonance spectroscopy31030109 nutrition & dieteticslcsh:QP1-981business.industryMagnesiumagingSkeletal muscleMuscle weaknessNuclear magnetic resonance spectroscopymedicine.diseaseP magnetic resonance spectroscopyEndocrinologymedicine.anatomical_structurechemistrySarcopeniamuscle strengthmedicine.symptombusinessIntracellular
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NMR Exchange Format: a unified and open standard for representation of NMR restraint data

2015

SCOPUS: le.j

0303 health sciencesElectronic Data ProcessingMagnetic Resonance SpectroscopyComputer sciencebusiness.industryeducationRepresentation (systemics)virus diseasesGénéralitésNuclear magnetic resonance spectroscopy010402 general chemistry01 natural sciencesArticle0104 chemical sciencesComputational science03 medical and health sciencesSoftwareNuclear magnetic resonanceStructural BiologyOpen standard[CHIM.ANAL]Chemical Sciences/Analytical chemistrybusinessMolecular BiologySoftware030304 developmental biologyNature structural & molecular biology
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1H, 13C, and 15N NMR chemical shift assignment of the complex formed by the first EPEC EspF repeat and N-WASP GTPase binding domain

2021

AbstractLEE-encoded effector EspF (EspF) is an effector protein part of enteropathogenic Escherichia coli’s (EPEC’s) arsenal for intestinal infection. This intrinsically disordered protein contains three highly conserved repeats which together compose over half of the protein’s complete amino acid sequence. EPEC uses EspF to hijack host proteins in order to promote infection. In the attack EspF is translocated, together with other effector proteins, to host cell via type III secretion system. Inside host EspF stimulates actin polymerization by interacting with Neural Wiskott-Aldrich syndrome protein (N-WASP), a regulator in actin polymerization machinery. It is presumed that EspF acts by di…

030303 biophysicsRegulatormacromolecular substancesBiochemistryArticleType three secretion system03 medical and health sciencesStructural BiologyEnteropathogenic Escherichia coliNMR-spektroskopiaN-WASPPeptide sequenceActin030304 developmental biologysolution NMRSolution NMR0303 health sciencesEffectorChemistryResonance assignmentsresonance assignmentsNuclear magnetic resonance spectroscopyintrinsically disordered protein3. Good healthCell biologytype III secretion systemType III secretion systemIntrinsically disordered proteinEPEC EspFproteiinitGTPase bindingBiomolecular Nmr Assignments
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Structural analysis of Cu(II) ligation to the 5'-GMP nucleotide by pulse EPR spectroscopy.

2007

JBIC Journal of Biological Inorganic Chemistry, 12 (6)

10120 Department of ChemistryConformational change1303 BiochemistryAnalytical chemistryGuanosine MonophosphateLigandsBiochemistrylaw.inventionInorganic Chemistrycopper; electron-nuclear double resonance; hyperfine sublevel correlation spectroscopy; pulse electron paramagnetic resonance spectroscopy; nucleotidelaw540 ChemistryOrganometallic CompoundsDNA Z-FormElectron paramagnetic resonanceHyperfine structurehyperfine sublevel correlation spectroscopyElectron nuclear double resonanceMolecular StructurePulsed EPRChemistryLigand1604 Inorganic ChemistryElectron Spin Resonance SpectroscopyDNAnucleotideSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)CrystallographyUnpaired electronpulse electron paramagnetic resonance spectroscopyNucleic Acid Conformationelectron-nuclear double resonanceTwo-dimensional nuclear magnetic resonance spectroscopyCopperJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry
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Crystal and solution structures of di-n-butyltin(IV) complexes of 5-[(E)-2-(4-methoxyphenyl)-1-diazenyl]quinolin-8-ol and benzoic acid derivatives: E…

2009

Abstract Reactions of nBu2SnCl(L1) (1), where L1 = acid residue of 5-[(E)-2-(4-methoxyphenyl)-1-diazenyl]quinolin-8-ol, with various substituted benzoic acids in refluxing toluene, in the presence of triethylamine, yielded dimeric mixed ligand di-n-butyltin(IV) complexes of composition [nBu2Sn(L1)(L2–6)]2 where L2 = benzene carboxylate (2), L3 = 2-[(E)-2-(2-hydroxy-5-methylphenyl)-1-diazenyl]benzoate (3), L4 = 5-[(E)-2-(4-methylphenyl)-1-diazenyl]-2-hydroxybenzoate (4), L5 = 2-{(E)-4-hydroxy-3-[(E)-4-chlorophenyliminomethyl]-phenyldiazenyl}benzoate (5) and L6 = 2-[(E)-(3-formyl-4-hydroxyphenyl)-diazenyl]benzoate (6). All complexes (1–6) have been characterized by elemental analyses, IR, 1H,…

10120 Department of Chemistry[(E)81303 Biochemistry5DenticityStereochemistry12Crystal structuredinBiochemistrybutyltin(IV) complexes(4Inorganic Chemistrychemistry.chemical_compoundPentagonal bipyramidal molecular geometry540 ChemistryMaterials ChemistryCarboxylatePhysical and Theoretical Chemistry2505 Materials ChemistryCoordination geometryXmixed ligandsol1604 Inorganic ChemistryChemistryCrystal structurebenzoic acidOrganic Chemistry5-[(E)-2-(4-methoxyphenyl)-1- diazenyl]quinolin-8-ol Di-n-butyltin(IV) complexes Benzoic acid Mixed ligands Solution and solid-state tin NMR Crystal structureNuclear magnetic resonance spectroscopysolution and solid state tinNMRBond lengthTrigonal bipyramidal molecular geometryCrystallographydiazenyl]quinolinmethoxyphenyl)Settore CHIM/03 - Chimica Generale E Inorganica1606 Physical and Theoretical Chemistry1605 Organic Chemistry
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