Search results for "Random hexamer"

showing 10 items of 16 documents

Ab initio determination of the ionization potentials of water clusters (H2O)n (n = 2-6).

2012

High-level quantum-chemical ab initio coupled-cluster and multiconfigurational perturbation methods have been used to compute the vertical and adiabatic ionization potentials of several water clusters: dimer, trimer, tetramer, pentamer, hexamer book, hexamer ring, hexamer cage, and hexamer prism. The present results establish reference values at a level not reported before for these systems, calibrating different computational strategies and helping to discard less reliable theoretical and experimental data. The systematic study with the increasing size of the water cluster allows obtaining some clues on the structure and reductive properties of liquid water.

010304 chemical physicsPentamerDimerAb initioGeneral Physics and AstronomyTrimerRandom hexamer010402 general chemistry01 natural sciencesMolecular physics0104 chemical scienceschemistry.chemical_compoundchemistryAb initio quantum chemistry methodsIonization0103 physical sciencesPhysics::Atomic and Molecular ClustersWater clusterPhysical and Theoretical ChemistryAtomic physicsThe Journal of chemical physics
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Structures of collagen IV globular domains: insight into associated pathologies, folding and network assembly

2018

15 páginas, 6 figuras, 1 tabla.

0301 basic medicineGoodpasture’s diseaseAddenda and ErrataRandom hexamerBiochemistryEpitopelaw.invention03 medical and health sciencesAlport's syndrome0302 clinical medicineGoodpasture's diseaselawMissense mutationGeneral Materials ScienceAlport’s syndromeStructural motifNetwork assemblyCrystallographyGoodpasture's diseaseChemistry(IV)NC1 hexamersStructural proteinCollagen type IVGeneral ChemistryCondensed Matter PhysicsResearch PapersFolding (chemistry)030104 developmental biologyQD901-999BiophysicsRecombinant DNA030217 neurology & neurosurgeryAlport syndrome
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Quaternary and subunit structure of Calliphora arylphorin as deduced from electron microscopy, electrophoresis, and sequence similarities with arthro…

1992

Arylphorin was purified from larvae of the blowfly Calliphora vicina and studied in its oligomeric form and after dissociation at pH 9.6 into native subunits. In accordance with earlier literature, it was electrophoretically shown to be a 500 kDa hexamer (1 x 6) consisting of 78 kDa polypeptides (= subunits). Electron micrographs of negatively stained hexamers show a characteristic curvilinear, equilateral triangle of 12 nm in diameter (top view) and a rectangle measuring 10 x 12 nm (side view). Alternatively, particles in the top view orientation exhibit a roughly circular shape 12 nm in diameter. Crossed immunoelectrophoresis revealed the presence of a major subunit type; the nature of a …

Insectaanimal structuresCalliphora vicinaProtein ConformationPhysiologyStereochemistryProtein subunitmedicine.medical_treatmentMolecular Sequence DataBiologyRandom hexamerBiochemistryCalliphoraEndocrinologyHemolymphmedicineAnimalsAmino Acid SequenceEcology Evolution Behavior and SystematicsGlycoproteinsSequence Homology Amino AcidProtein primary structureSpidersHemocyaninbiology.organism_classificationNephropidaeMicroscopy ElectronBiochemistryInsect HormonesLarvaHemocyaninsInsect ProteinsElectrophoresis Polyacrylamide GelAnimal Science and ZoologyProtein quaternary structureJournal of Comparative Physiology B
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Tryptophan quenching as linear sensor for oxygen binding of arthropod hemocyanins.

2008

Oxygen binding of hemocyanins results in an absorption band around 340nm and a strong quenching of the intrinsic tryptophan fluorescence. Our study analyses in detail the fluorescence quenching within two hemocyanins, a hexamer (Panulirus interruptus) and a 4 x 6-mer (Eurypelma californicum). Based on the comparison of calculated and measured transfer efficiencies we could show that: (1) For both hemocyanins FRET (fluorescence resonance energy transfer) is exclusively responsible for quenching of the tryptophan fluorescence upon oxygen binding. (2) Tryptophan quenching by FRET is independent of the oxy- or deoxy conformation of the protein. (3) The quenching takes place at the subunit level…

Models MolecularBiophysicschemistry.chemical_elementBiosensing TechniquesRandom hexamerPhotochemistryBiochemistryOxygenAbsorptionProtein structureAnimalsProtein Structure QuaternaryMolecular BiologyArthropodsQuenching (fluorescence)ChemistryTryptophanTryptophanFluorescenceOxygenFörster resonance energy transferSpectrometry FluorescenceEnergy TransferHemocyaninsOxygen bindingProtein BindingBiochimica et biophysica acta
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All hierarchical levels are involved in conformational transitions of the 4×6-meric tarantula hemocyanin upon oxygenation

2002

The respiratory protein of the tarantula Eurypelma californicum is a 4 x 6-meric hemocyanin that binds oxygen with high cooperativity. This requires the existence of different conformations which have been confirmed by small angle X-ray scattering (SAXS). Here we present reconstructed 3D-models of the oxy- and deoxy-forms of tarantula hemocyanins, as obtained by fitting small angle X-rays scattering curves on the basis of known X-ray structures and electron microscopy of related hemocyanins. For the first time, the involvement of movements at all levels of the quaternary structure was confirmed for an arthropod hemocyanin upon oxygenation. The two identical 2 x 6-meric half-molecules of the…

Models MolecularMacromolecular SubstancesProtein Conformationmedicine.medical_treatmentAllosteric regulationBiophysicsCooperativityRandom hexamerBiochemistryOligomerAnalytical Chemistrychemistry.chemical_compoundmedicineAnimalsMolecular BiologySmall-angle X-ray scatteringSpidersHemocyaninOxygenRespiratory proteinCrystallographychemistryHemocyaninsProtein quaternary structureOxidation-ReductionProtein BindingBiochimica et Biophysica Acta (BBA) - Proteins and Proteomics
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NMR study of hexanucleotide d(CCGCGG)2 containing two triplet repeats of fragile X syndrome

2003

Abstract Long repeated stretches of d(CCG) and tri-nucleotide are crucial mutations that cause hereditary forms of mental retardation (fragile X-syndrome). Moreover, the alternating (CG) di-nucleotide is one of the candidates for Z-DNA conformation. Solution NMR structure of d(CCGCGG) 2 has been solved and is discussed. The determined NMR solution structure is a distorted highly bent B-DNA conformation with increased flexibility in both terminal residues. This conformation differs significantly from the Z-DNA tetramer structure reported for the same hexamer in the crystal state at similar ionic strength by Malinina and co-workers. Crystal structure of d(CCGCGG) 2 at high salt concentration …

Models MolecularMagnetic Resonance SpectroscopyOligonucleotidesBiophysicsCrystal structureRandom hexamerRing (chemistry)Biochemistrychemistry.chemical_compoundTetramerNucleic AcidsHumansMoleculeComputer SimulationMolecular BiologyRecombination Geneticchemistry.chemical_classificationChemistryDNACell BiologyFuranoseCrystallographyIonic strengthFragile X SyndromeNucleic Acid ConformationTrinucleotide Repeat ExpansionCytosineBiochemical and Biophysical Research Communications
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Cockroach allergens Per a 3 are oligomers

2009

Allergens from cockroaches cause major asthma-related health problems worldwide. Among them Per a 3 belongs to the most potent allergens. Although the sequences of some members of the Per a 3-family are known, their biochemical and biophysical properties have not been investigated. Here we present for the first time a thorough structural characterization of these allergens, which have recently been tested to induce an increase of allergy specific indicators in blood of Europeans. We isolated two Per a 3 isoforms, which occur freely dissolved in the hemolymph as hexamers with molecular masses of 465+/-25kDa (P II) and 512+/-25kDa (P I). Their sedimentation coefficients (S(20,W)) were determi…

Models MolecularSequence analysismedicine.medical_treatmentProtein subunitMolecular Sequence DataImmunologySequence alignmentRandom hexamermedicine.disease_causeMass SpectrometryAllergenmedicineAnimalsPeriplanetaProtein IsoformsAmino Acid SequencePeptide sequenceBase SequencebiologyCircular DichroismHemocyaninSequence Analysis DNAAllergensbiology.organism_classificationMicroscopy ElectronMicroscopy FluorescenceBiochemistryImmunologyInsect ProteinsElectrophoresis Polyacrylamide GelAmerican cockroachSequence AlignmentUltracentrifugationDevelopmental BiologyDevelopmental & Comparative Immunology
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Complete Sequence of the 24-mer Hemocyanin of the TarantulaEurypelma californicum

2000

Hemocyanins are large oligomeric respiratory proteins found in many arthropods and molluscs. The hemocyanin of the tarantula Eurypelma californicum is a 24-mer protein complex with molecular mass of 1,726,459 Da that consists of seven different polypeptides (a–g), each occupying a distinct position within the native molecule. Here we report the complete molecular structure of the E. californicumhemocyanin as deduced from the corresponding cDNAs. This represents the first complex arthropod hemocyanin to be completely sequenced. The different subunits display 52–66% amino acid sequence identity. Within the subunits, the central domain, which bears the active center with the copper-binding sit…

Molecular massStereochemistryProtein subunitmedicine.medical_treatmentHemocyaninCell BiologyAnatomyBiologyRandom hexamerBiochemistryComplete sequencePhylogeneticsmedicineHomology modelingMolecular BiologyPeptide sequenceJournal of Biological Chemistry
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Spin-coupling topology in the copper hexamer compounds A2Cu3O(SO4)3 (A=Na, K)

2020

The compounds ${A}_{2}\mathrm{C}{\mathrm{u}}_{3}\mathrm{O}{(\mathrm{S}{\mathrm{O}}_{4})}_{3}$ $(A=\mathrm{Na},\phantom{\rule{0.16em}{0ex}}\mathrm{K})$ are characterized by copper hexamers that are weakly coupled to realize antiferromagnetic order below ${T}_{N}\ensuremath{\approx}3\phantom{\rule{0.16em}{0ex}}\mathrm{K}$. They constitute quantum spin systems with $S=1$ triplet ground states. We investigated the energy-level splittings of the copper hexamers by inelastic neutron scattering experiments covering the entire range of the magnetic excitation spectra. The observed transitions are governed by very unusual selection rules that we ascribe to the underlying spin-coupling topology. This…

PhysicsExcitation spectrachemistry.chemical_elementOrder (ring theory)Coupling topology02 engineering and technologyRandom hexamer021001 nanoscience & nanotechnology01 natural sciencesCopperInelastic neutron scatteringCrystallographychemistry0103 physical sciencesAntiferromagnetism010306 general physics0210 nano-technologySpin (physics)Physical Review B
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Entrapment of amino acids in gas phase surfactant assemblies: The case of tryptophan confined in positively charged (1R,2S)-dodecyl (2-hydroxy-1-meth…

2017

The ability of positively charged aggregates of the surfactant (1R,2S)‐dodecyl (2‐hydroxy‐1‐methyl‐2‐phenylethyl))dimethylammonium bromide (DMEB) to incorporate D-tryptophan or L-tryptophan in the gas phase has been investigated by electrospray ion mobility mass spectrometry (ESI‐IM‐MS). Strongly impacted by the pH of the electrosprayed solutions, both protonated (T+) and deprotonated (T-) tryptophan are effectively included into the aggregates, whereas, tryptophan in zwitterionic (T0) form is practically absent in singly charged DMEB aggregates but can be found in multiply charged ones. The ability to incorporate tryptophan increases with the aggregation number and charge state of aggr…

Spectrometry Mass Electrospray IonizationSurfactant aggregateCollision-induced dissociationIon mobilityMolecular ConformationProtonationRandom hexamerGas-phase self-assembly010402 general chemistryPhotochemistry01 natural sciencesGas‐phase self‐assemblychemistry.chemical_compoundSurface-Active AgentsDeprotonationBromideCationsOrganic chemistryMoietyDMEBSpectroscopyAggregation number010401 analytical chemistryTryptophanTryptophanStereoisomerism0104 chemical sciencesQuaternary Ammonium CompoundschemistryGasesJournal of mass spectrometry : JMS
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