Search results for "Disulfide"

showing 10 items of 171 documents

CCDC 263593: Experimental Crystal Structure Determination

2005

Related Article: A.Laromaine, F.Teixidor, R.Kivekas, R.Sillanpaa, R.Benakki, B.Gruner, C.Vinas|2005|Dalton Trans.||1785|doi:10.1039/b502328a

Space GroupCrystallographyCrystal SystemCrystal StructureCell Parametersbis(2-methyl-12-dicarba-closo-dodecaboranyl)disulfideExperimental 3D Coordinates
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CCDC 980426: Experimental Crystal Structure Determination

2014

Related Article: Almudena Gallego, Oscar Castillo, Carlos J. Gómez-García, Félix Zamora, Salome Delgado|2014|Eur.J.Inorg.Chem.||3879|doi:10.1002/ejic.201400085

Space GroupCrystallographyCrystal SystemCrystal StructureCell Parameterscatena-((mu2-Bromo)-(mu2-bis(2-pyrimidyl)disulfide)-copper(i) acetonitrile solvate)Experimental 3D Coordinates
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CCDC 660922: Experimental Crystal Structure Determination

2010

Related Article: M.Ohba, K.Yoneda, G.Agusti, M.C.Munoz, A.B.Gaspar, J.A.Real, M.Yamasaki, H.Ando, Y.Nakao, S.Sakaki, S.Kitagawa|2009|Angew.Chem.,Int.Ed.|48|4767|doi:10.1002/anie.200806039

Space GroupCrystallographyCrystal SystemCrystal StructureCell Parameterscatena-[tetrakis(mu~2~-Cyano)-(mu~2~-pyrazine)-iron(ii)-platinum(ii) carbon disulfide clathrate]Experimental 3D Coordinates
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CCDC 775642: Experimental Crystal Structure Determination

2011

Related Article: C.J.Adams, J.A.Real, R.E.Waddington|2010|CrystEngComm|12|3547|doi:10.1039/c0ce00149j

Space GroupCrystallographyCrystal Systemcatena-(bis(mu~2~-44'-Bipyridine)-di-isothiocyanato-iron(ii) carbon disulfide solvate)Crystal StructureCell ParametersExperimental 3D Coordinates
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CCDC 263594: Experimental Crystal Structure Determination

2005

Related Article: A.Laromaine, F.Teixidor, R.Kivekas, R.Sillanpaa, R.Benakki, B.Gruner, C.Vinas|2005|Dalton Trans.||1785|doi:10.1039/b502328a

Space GroupCrystallographybis(2-phenyl-12-dicarba-closo-dodecaboranyl)disulfideCrystal SystemCrystal StructureCell ParametersExperimental 3D Coordinates
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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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