Search results for "Disulfides"

showing 10 items of 54 documents

Expression and glycosylation studies of human FGF receptor 4

2001

Fibroblast growth factor receptor subtype 4 (FGFR4) has been shown to have special activation properties and just one splicing form, unlike the other FGFRs. FGFR4 overexpression is correlated with breast cancer and therefore FGFR4 is a target for drug design. Our aim is to overexpress high amounts of homogeneous FGFR4 extracellular domain (FGFR4ed) for structural studies. We show that baculovirus-insect cell-expressed FGFR4ed is glycosylated on three (N88, N234, and N266) of the six possible N-glycosylation sites but is not O-glycosylated. The deglycosylated triple mutant was expressed and had binding properties similar to those of glycosylated FGFR4ed, but was still heterogeneous. Large am…

Protein FoldingGlycosylationGlycosylationBlotting WesternImmunoblottingMolecular Sequence DataProtein RenaturationBiologyFibroblast growth factorMass SpectrometryInclusion bodiesCell Line03 medical and health scienceschemistry.chemical_compoundSDG 3 - Good Health and Well-beingEscherichia coliAnimalsHumansReceptor Fibroblast Growth Factor Type 4TrypsinAmino Acid SequenceDisulfidesReceptorChromatography High Pressure Liquid030304 developmental biologyInclusion Bodies0303 health sciencesHeparin030302 biochemistry & molecular biologyFibroblast growth factor receptor 4Fibroblast growth factor receptor 3Receptors Fibroblast Growth FactorMolecular biologyRecombinant Proteins3. Good healthchemistryFibroblast growth factor receptorMutationRNA splicing/dk/atira/pure/sustainabledevelopmentgoals/good_health_and_well_beingBaculoviridaeBiotechnology
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Identification of disulphide bonds in the refolding of bovine pancreatic RNase A

1996

Background: Comprehension of the rules that govern the folding process is still far from satisfactory, though it is nevertheless clear that all the information required to define the folding is encoded in the amino acid sequence. In proteins that contain disulphide bonds, folding is associated with disulphide bond formation. Protein species with different numbers of disulphides tend to accumulate during the process; these species can be trapped in a stable form, by quenching any remaining free SH groups, and then characterized in order to identify the disulphide bonds formed. Results The refolding pathway of reduced and denatured RNase A has been studied using mass spectrometric strategies …

Protein FoldingSh groupsRNase P010402 general chemistryPeptide Mapping01 natural sciencesBiochemistryrefolding03 medical and health sciencesRNase AAnimalsDisulfidesES-MSPeptide sequencedisulphide bonds030304 developmental biology0303 health sciencesQuenching (fluorescence)ChemistryFAB-MSRibonuclease Pancreatic0104 chemical sciencesFolding (chemistry)CrystallographyMolecular MedicineCattlePancreatic RNaseDisulphide bondsCysteineFolding and Design
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Control of the ribulose 1,5-bisphosphate carboxylase/oxygenase activity by the chloroplastic glutathione pool.

2014

The CO2-fixing activity of ribulose 1,5-bisphosphate carboxylase/oxygenase depends on the redox state of its cysteines. Disulfides like cystamine or 5,5'-dithio-bis(2-nitrobenzoic acid), but not oxidized glutathione, switch the enzyme to the inactive oxidized form. Conversely, thiols like cysteamine, cysteine, dithiotreitol or 2-mercaptoethanol, but not reduced glutathione, recover enzymatic activity after a previous oxidation. Direct regulation of the carboxylase activity by the chloroplastic glutathione pool is hindered by kinetic barriers impeding access to the critical residues. However, reduced glutathione can drive the recovery of activity by means of minute amounts of smaller interme…

Ribulose 15-bisphosphateChloroplastsGPX3ChemistryRibuloseRibulose-Bisphosphate CarboxylaseGlutathione reductaseBiophysicsCystamineGlutathioneBiochemistryGlutathionePyruvate carboxylaseEnzyme Activationchemistry.chemical_compoundBiochemistryGlutaredoxinDisulfidesSulfhydryl CompoundsMolecular BiologyChlamydomonas reinhardtiiCysteineArchives of biochemistry and biophysics
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Composition of the essential oil of allium neapolitanum cirillo growing wild in sicily and its activity on microorganisms affecting historical art cr…

2015

Essential oil of the aerial parts of Allium neapolitanum Cirillo collected in Sicily were analyzed by gas-chromatography-flame-ionization detection and gas-chromatography-mass spectrometry. Nineteen compounds were identified in the oil and the main components were found to be (E)-chrysanthenyl acetate (28.1%), (Z)-chrysanthenyl acetate (23.8%), (E)-β-farnesene (9.6%), dimethyl trisulfide (9.6%), camphor (7.4%), methyl allyl disulfide (6.8%) and 1-methyl-3-allyl trisulfide (5.8%). The essential oil showed good antimicrobial activity against 11 strains of test microorganisms, including several species infesting historical material.

SesquiterpeneGeneral Chemical EngineeringAllyl compoundMonoterpeneAntimicrobial activityPlant OilEssential oillaw.inventionCamphorchemistry.chemical_compoundlaw(E)-chrysanthenyl acetateChemical Engineering (all)DisulfidesFood scienceMedicinal plantsSicilyFlame IonizationbiologyChemistry (all)food and beveragesGeneral MedicineAntimicrobialAllyl CompoundsArtifactAlliumArtifactsSesquiterpenesArt(Z)-chrysanthenyl acetateSulfideAllium neapolitanumSulfidesGas Chromatography-Mass SpectrometryAlliumBridged Bicyclo CompoundsDisulfideDrug Resistance FungalBotanyDrug Resistance BacterialOils VolatilePlant OilsAllium neapolitanumEssential oilBacteriaFungiGeneral ChemistryPlant Components Aerialbiology.organism_classificationCamphorchemistryMonoterpenesBridged Bicyclo CompoundDimethyl trisulfideAllyl Compound
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Programmed Formation of HCN Oligomers through Organosulfur Catalysis

2021

An efficient, inexpensive, and reliable synthesis of diaminomaleonitrile (DAMN, 1) is described starting from readily available acetone cyanohydrin as the source of hydrogen cyanide (HCN). Diaminomaleonitrile (DAMN) is known to be an important intermediate in heterocyclic and medicinal chemistry as well as being a possible precursor for the origin of life's hypothesis within prebiotic chemistry. The mechanism of its formation through organosulfur catalysis has been investigated by electrospray ionization mass spectrometry (ESI-MS) using two newly synthesized cationic "marker" molecules as a tool that allows for sensitive detection. As a result, the proposed mechanism of a thiocyanate-mediat…

Spectrometry Mass Electrospray IonizationChemistry PharmaceuticalElectrospray ionizationOrganic ChemistryCationic polymerizationCombinatorial chemistryCatalysisCatalysischemistry.chemical_compoundchemistryTetramerDiaminomaleonitrileMoleculeDisulfidesOrganosulfur compoundsAcetone cyanohydrinThe Journal of Organic Chemistry
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Detection and localisation of disulphide bonds in a synthetic peptide reproducing the sequence 1-30 of Par j 1.0101 by electrospray ionisation mass s…

2001

The structural characterisation of a synthetic peptide reproducing the sequence 1–30 of Par j 1.0101, a major allergenic protein present in the pollen of Parietaria judaica, by combined use of chemical and enzymatic cleavage, reversed-phase high-performance liquid chromatography (RP-HPLC) and electrospray ionisation mass spectrometry (ESI-MS), is described. Direct ESI-MS of the synthetic peptide after reaction with methyl iodide showed that the product is a mixture of two peptides: one form in which two out of the four cysteine residues present in the sequence are oxidised and a minor amount of another form in which all the cysteines are fully reduced. It was ascertained, using the combined…

Spectrometry Mass Electrospray IonizationElectrospray ionisation mass spectrometrySettore CHIM/10 - Chimica Degli AlimentiMolecular Sequence Data010401 analytical chemistryReproducibility of ResultsDisulphide bridgesGeneral Medicine010402 general chemistryPeptide Mapping01 natural sciencesAtomic and Molecular Physics and OpticsParietaria judaica0104 chemical sciencessynthetic peptide; Par j 1.0101; Parietaria judaica; disulphide bridges; structural characterisation; electrospray ionisation mass spectrometrySynthetic peptideTrypsinAmino Acid SequenceCyanogen BromideDisulfidesStructural characterisationPeptidesPar j 1.0101Chromatography High Pressure LiquidSpectroscopy
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Characterization of heat-labile toxin-subunit B from Escherichia coli by liquid chromatography-electrospray ionization-mass spectrometry and matrix-a…

2012

The possibilities of characterizing the heat-labile enterotoxin (LT) of enterotoxigenic Escherichia coli (ETEC) by liquid chromatography electrospray mass spectrometry (LC/ESI-MS) and matrix-assisted laser desorption with time-of-flight mass spectrometry (MALDI-TOF-MS) were investigated. The B subunit from recombinant E. coli (expression in Pichia pastoris) can be detected by LC/ESI-MS expressed in P. pastoris and the charge envelope signals can be observed; LC/ESI-MS and MALDI-TOF-MS analysis allowed the acquisition of labile toxin subunit B (LTB) molecular weight and preliminary structural characterization of LTB toxin. MALDI-TOF analysis after reduction and alkylation of the protein evid…

Spectrometry Mass Electrospray IonizationElectrospray ionizationProtein subunitBacterial ToxinsMolecular Sequence DataToxicologyMass spectrometrymedicine.disease_causespettroemtria di massaPichiaPichia pastorisEnterotoxinsProtein sequencingEnterotoxigenic Escherichia colimedicineTrypsinAmino Acid SequenceDisulfidesPhosphorylationEscherichia colitossinaChromatographyMolecular massbiologyChemistryEscherichia coli ProteinsE. coliGeneral Medicinebiology.organism_classificationRecombinant ProteinsMolecular WeightProtein SubunitsSpectrometry Mass Matrix-Assisted Laser Desorption-IonizationFood ScienceChromatography LiquidFood and chemical toxicology : an international journal published for the British Industrial Biological Research Association
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Rethinking Cysteine Protective Groups:S-Alkylsulfonyl-l-Cysteines for Chemoselective Disulfide Formation

2016

The ability to reversibly cross-link proteins and peptides grants the amino acid cysteine its unique role in nature as well as in peptide chemistry. We report a novel class of S-alkylsulfonyl-l-cysteines and N-carboxy anhydrides (NCA) thereof for peptide synthesis. The S-alkylsulfonyl group is stable against amines and thus enables its use under Fmoc chemistry conditions and the controlled polymerization of the corresponding NCAs yielding well-defined homo- as well as block co-polymers. Yet, thiols react immediately with the S-alkylsulfonyl group forming asymmetric disulfides. Therefore, we introduce the first reactive cysteine derivative for efficient and chemoselective disulfide formation…

Stereochemistry010402 general chemistryCleavage (embryo)01 natural sciencesRing-opening polymerizationCatalysisAnhydridesPolymerizationchemistry.chemical_compoundPeptide synthesisCysteineDisulfidesSulfhydryl CompoundsAmineschemistry.chemical_classification010405 organic chemistryOrganic ChemistryGeneral Chemistry0104 chemical sciencesAmino acidchemistryPolymerizationDrug deliveryPeptidesDerivative (chemistry)CysteineChemistry - A European Journal
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Coupling of the heme and an internal disulfide bond in human neuroglobin

2004

Neuroglobin displays a hexacoordination His-Fe-His in the absence of external ligands such as oxygen. The observed oxygen affinity therefore depends on the binding rates of both oxygen and the competing distal histidine. Furthermore, the binding properties depend on the presence of an internal disulfide bond. In the case of human neuroglobin, cysteines at positions CD7 and D5 are sufficiently close to form an internal disulfide bond. For cytoglobin, the cysteine residues at positions A7 and GH4 may also form a disulfide bond. Mass spectrometry, ligand binding, and thiol accessibility studies were used to study the role influence of these disulfide bonds. Mutation of specific cysteines, or r…

StereochemistryNeuroglobinGeneral Physics and Astronomychemistry.chemical_elementNerve Tissue ProteinsHemeOxygenMass Spectrometrychemistry.chemical_compoundStructural BiologyHumansGeneral Materials ScienceCysteineDisulfidesHemeHistidinechemistry.chemical_classificationCytoglobinCell BiologyGlobinsOxygenchemistryBiochemistryNeuroglobinThiolOxygen bindingCysteineMicron
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An Atom-Economical Approach to Functionalized Single-Walled Carbon Nanotubes: Reaction with Disulfides

2013

Owing to their unique structure, thermal stability, and mechanical and electronic properties, single-walled carbon nanotubes (SWCNTs) have been a subject of continuous and intense interest. However, various applications in many fields, such as molecular electronics, solar cells, and nanomedicine, often require the development of reproducible protocols for the chemical modification of SWCNTs. In fact, one of the main drawbacks of the use of SWCNTs is their tendency to aggregate and intrinsic poor solubility, which prevent their manipulation and limit their potential. To date, several methods have been described for the chemical functionalization of SWCNTs; however, new versatile and reliable…

atom economydisulfidesCarbon NanotubeInorganic chemistryOrganic Functionalization02 engineering and technologyCarbon nanotubedendrimer010402 general chemistry01 natural sciencesCatalysisdendrimerslaw.inventionchemistry.chemical_compoundlawAtom economyDendrimerThermal stabilitycarbon nanotubeCarbon Nanotubes; Organic FunctionalizationDiphenyl disulfidecarbon nanotubesMolecular electronicsGeneral MedicineSettore CHIM/06 - Chimica OrganicaGeneral Chemistry021001 nanoscience & nanotechnologyCombinatorial chemistry0104 chemical scienceschemistryfunctionalizationSurface modification0210 nano-technologydisulfideCarbon monoxide
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