Search results for " quaternary s"

showing 10 items of 46 documents

Quaternary structure and molecular model of a 4x6mer arthropod hemocyanin in oxygenated and deoxygenated states by 3D cryo-electron microscopy

2007

Extended abstract of a paper presented at MC 2007, 33rd DGE Conference in Saarbrücken, Germany, September 2 – September 7, 2007

CrystallographyMolecular modelbiologyChemistryCryo-electron microscopymedicine.medical_treatmentBiophysicsmedicineProtein quaternary structureHemocyaninArthropodbiology.organism_classificationInstrumentationMicroscopy and Microanalysis
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Quaternary transition pathway in sol–gel encapsulated haemoglobin tracked by NIR and UV spectral relaxations

2008

→T structural transition of haemoglobin (hb), the protein responsible for oxygen (o) transport in the red blood cells of vertebrates, is the hall mark example. This transition, which regu lates o2 uptake in the lungs and o2 release in the tissues, is a switch in the quaternary structure of the protein from a low-affinity state (T) to a high-affinity state (R), two well-characterised structures. The struc tural pathway connecting the end states of this transition remains unclear, however, although recently several experimental 1 or

CrystallographyTransition (genetics)quaternary relaxationChemistryStereochemistryprotein dynamicchemistry.chemical_elementProtein quaternary structureStructural transitionQuaternaryOxygensol-gel encapsulationSol-gel
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The SARS-CoV-2 envelope (E) protein has evolved towards membrane topology robustness.

2021

- Single-spanning SARS-CoV-2 envelope (E) protein topology is a major determinant of protein quaternary structure and function. - Charged residues distribution in E protein sequences from highly pathogenic human coronaviruses (i.e., SARS-CoV, MERS-CoV and SARS-CoV-2) stabilize Ntout-Ctin membrane topology. - E protein sequence could have evolved to ensure a more robust membrane topology from MERS-CoV to SARS-CoV and SARS-CoV-2.

EvolutionvirusesBiophysicsBBA Research Lettermedicine.disease_causeBiochemistryEnvelope proteinCell membraneEvolution Molecular03 medical and health sciencesCoronavirus Envelope ProteinsProtein sequencingmedicineHumansskin and connective tissue diseasesProtein Structure Quaternary030304 developmental biologyCoronavirus0303 health sciencesChemistrySARS-CoV-2030302 biochemistry & molecular biologyfungiCell MembraneRobustness (evolution)virus diseasesCell Biologyrespiratory tract diseasesCoronavirusmedicine.anatomical_structureMembrane topologyMembrane topologyBiophysicsProtein quaternary structureProtein topologyFunction (biology)Biochimica et biophysica acta. Biomembranes
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Spectroscopic markers of the T-R quaternary transition in human hemoglobin

2004

n questo lavoro, usiamo un protocollo sol-gel per intrappolare e confrontare gli stati quaternari R e T di entrambi i deossigenati (deossiHb) ederivati ​​di ossido di carbonio (HbCO) dell'emoglobina umana. La banda di assorbimento ottico del vicino infrarosso III e lo stretching di CO a infrarossibanda sono utilizzati per rilevare l'effetto della struttura quaternaria sulle proprietà spettrali di deoxyHb e HbCO; confronto con mioglobinaconsente una valutazione dei contributi terziari e quaternari ai turni di banda misurati. La RXLa transizione T è indicata per causare un bluspostamento della banda III di ~ 35 cm?1per deoxyHb e uno spostamento rosso della banda di allungamento CO di soli ~ 0…

InfraredBiophysicsAnalytical chemistryBiochemistryPhase Transitionchemistry.chemical_compoundHemoglobinsSpectroscopy Fourier Transform InfraredHumansFourier transform infrared spectroscopySpectroscopyProtein Structure QuaternaryCarbon MonoxideChemistryOrganic ChemistryNear-infrared spectroscopyBand IIILow temperature spectroscopyTemperatureBand IIICO stretching bandOxygenSol–gel encapsulationCrystallographyKineticsFTIR spectroscopyMyoglobinAbsorption bandProtein quaternary structureBiomarkersProtein Binding
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Small angle neutron scattering study of the quaternary structure of haemocyanin of Rapana thomasiana

1996

Abstract Small angle neutron scattering (SANS) experiments were performed on a series of solutions of haemocyanin (Hc) of Rapana thomasiana . In a first series of solutions, by changing the external contrast a model of the molecule that is apparently in disagreement with electron microscopy (EM) measurements was obtained. The apparent disagreement was resolved by performing experiments on a series of variable protein concentration solutions in D 2 O. The physical parameters of the model, extrapolated to zero concentration, are in excellent agreement with the EM results obtained on samples more dilute than those examined with SANS.

Inorganic ChemistryCrystallographyRapana thomasianaSeries (mathematics)ChemistryOrganic ChemistryAnalytical chemistryMoleculeProtein quaternary structureSmall-angle neutron scatteringProtein concentrationSpectroscopyAnalytical ChemistryJournal of Molecular Structure
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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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Tracking the structural dynamics of proteins in solution using time-resolved wide-angle X-ray scattering

2008

We demonstrate tracking of protein structural changes with time-resolved wide-angle X-ray scattering (TR-WAXS) with nanosecond time resolution. We investigated the tertiary and quaternary conformational changes of human hemoglobin under nearly physiological conditions triggered by laser-induced ligand photolysis. We also report data on optically induced tertiary relaxations of myoglobin and refolding of cytochrome c to illustrate the wide applicability of the technique. By providing insights into the structural dynamics of proteins functioning in their natural environment, TR-WAXS complements and extends results obtained with time-resolved optical spectroscopy and X-ray crystallography.

Materials scienceProtein ConformationCrystallography X-RayBiochemistrySensitivity and SpecificityArticlechemistry.chemical_compoundHemoglobinsProtein structureScattering RadiationSpectroscopyWide-angle X-ray scatteringMolecular Biologyprotein dynamics conformational changes hemoglobin myoglobin cytochrome cScatteringMyoglobinX-RaysResolution (electron density)Cytochromes cCell BiologyNanosecondMyoglobinchemistryChemical physicsProtein quaternary structuresense organsBiotechnology
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Introduction of histidine residues into avidin subunit interfaces allows pH-dependent regulation of quaternary structure and biotin binding

2003

AbstractIn order to turn the subunit association and biotin binding of avidin into pH-sensitive phenomena, we have replaced individually three amino acid residues in avidin (Met96, Val115 and Ile117) with histidines in the 1–3 interface, and in combination with a histidine conversion in the 1–2 interface (Trp110). The single replacements Met96His and Val115His in the 1–3 interface were found to have a clear effect on the quaternary structure of avidin, since subunit associations of these mutants became pH-dependent. The histidine replacement in the 1–2 interface affected the biotin-binding properties of the mutants, in particular reversibility of binding and protein–ligand complex formation…

Models MolecularBiotin bindingInsectaProtein subunitBiophysicsBiotinBiosensing TechniquesBiochemistryCell LineProtein structureStructural BiologyGeneticsAnimalsHistidinepH dependenceProtein Structure QuaternaryMolecular BiologyHistidinebiologyChemistryCell BiologyProtein engineeringHydrogen-Ion ConcentrationAvidinRecombinant ProteinsMolecular WeightProtein SubunitsSpectrometry FluorescenceAmino Acid SubstitutionBiochemistryBiotinylationBiophysicsbiology.proteinProtein quaternary structureProtein engineeringBaculoviridaeProtein BindingAvidinFEBS Letters
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Evolution of molluscan hemocyanin structures

2013

AbstractHemocyanin transports oxygen in the hemolymph of many molluscs and arthropods and is therefore a central physiological factor in these animals. Molluscan hemocyanin molecules are oligomers composed of many protein subunits that in turn encompass subsets of distinct functional units. The structure and evolution of molluscan hemocyanin have been studied for decades, but it required the recent progress in DNA sequencing, X-ray crystallography and 3D electron microscopy to produce a detailed view of their structure and evolution. The basic quaternary structure is a cylindrical decamer 35nm in diameter, consisting of wall and collar (typically at one end of the cylinder). Depending on th…

Models MolecularEvolutionProtein Conformationmedicine.medical_treatmentProtein subunitProtein Data Bank (RCSB PDB)BiophysicsCrystallography X-RayHemocyaninBiochemistryAnalytical ChemistryRespiratory proteinsPaleontologyHemolymphElectron microscopymedicineQuaternary structureAnimalsMolecular BiologybiologyHemocyanincomputer.file_formatKeyhole limpet hemocyaninProtein Data BankBiological EvolutionMolluscaEvolutionary biologyHemocyaninsbiology.proteinProtein quaternary structureKLHcomputerKeyhole limpet hemocyaninOxygen bindingBiochimica et Biophysica Acta (BBA) - Proteins and Proteomics
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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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