Search results for "Quaternary"

showing 10 items of 411 documents

Production of biologically active recombinant avidin in baculovirus-infected insect cells

1997

Abstract An efficient lepidopteran insect cell system was established for the expression of a recombinant form of chicken egg-white avidin. The gene product was obtained in both secreted and intracellular forms, and biologically active recombinant avidin was isolated using affinity chromatography on an iminobiotin–agarose column. Similar to the known quaternary structure of the native egg-white protein, the purified recombinant protein was glycosylated and assembled mainly into tetramers. Like native avidin, the recombinant tetramer also exhibited a high level of thermostability, and was further stabilized upon binding biotin. The biotin-binding and structural properties of the recombinant …

Protein DenaturationGlycosylationProtein ConformationGenetic VectorsBiotinEnzyme-Linked Immunosorbent AssaySpodopteraChromatography Affinitylaw.inventionchemistry.chemical_compoundAffinity chromatographyBiotinTetramerlawAnimalsbiologySepharoseAvidinFusion proteinRecombinant ProteinsBiochemistrychemistryBiotinylationRecombinant DNAbiology.proteinProtein quaternary structureBaculoviridaeChickensBiotechnologyAvidinProtein Expression and Purification
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Recombinant functional multidomain hemoglobin from the gastropod Biomphalaria glabrata

2011

The extracellular hemoglobin multimer of the planorbid snail Biomphalaria glabrata, intermediate host of the human parasite Schistosoma mansoni, is presumed to be a 1.44 MDa complex of six 240 kDa polypeptide subunits, arranged as three disulfide-bridged dimers. The complete amino acid sequence of two subunit types (BgHb1 and BgHb2), and the partial sequence of a third type (BgHb3) are known. Each subunit encompasses 13 paralogus heme domains, and N-terminally a smaller plug domain responsible for subunit dimerization. We report here the recombinant expression of different functional fragments of BgHb2 in Escherichia coli, and of the complete functional subunits BgHb1 and BgHb2 in insect ce…

Protein subunitClinical BiochemistryCooperativitymedicine.disease_causeBiochemistrylaw.inventionHemoglobinschemistry.chemical_compoundlawGeneticsmedicineAnimalsHumansBiomphalaria glabrataProtein Structure QuaternaryMolecular BiologyEscherichia coliPeptide sequenceHemeBiomphalariabiologySchistosoma mansoniCell Biologybiology.organism_classificationRecombinant ProteinsOxygenProtein SubunitsBiochemistrychemistryRecombinant DNAOxygen bindingIUBMB Life
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Three-dimensional structure of the anaphase-promoting complex.

2001

The anaphase-promoting complex (APC) is a cell cycle-regulated ubiquitin-protein ligase, composed of at least 11 subunits, that controls progression through mitosis and G1. Using cryo-electron microscopy and angular reconstitution, we have obtained a three-dimensional model of the human APC at a resolution of 24 A. The APC has a complex asymmetric structure 140 A x 140 A x 135 A in size, in which an outer protein wall surrounds a large inner cavity. We discuss the possibility that this cavity represents a reaction chamber in which ubiquitination reactions take place, analogous to the inner cavities formed by other protein machines such as the 26S proteasome and chaperone complexes. This cag…

Protein subunitUbiquitin-Protein LigasesAnaphase-Promoting Complex-CyclosomeLigasesProtein structureUbiquitinHumansProtein Structure QuaternaryMitosisMolecular Biologychemistry.chemical_classificationDNA ligasebiologyCryoelectron MicroscopyG1 PhaseUbiquitin-Protein Ligase ComplexesCell BiologyPrecipitin TestsCell biologyProtein Structure TertiaryProteasomechemistryChaperone (protein)biology.proteinAnaphase-promoting complexHeLa CellsMolecular cell
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Heat shock protein 27 is involved in SUMO-2/3 modification of heat shock factor 1 and thereby modulates the transcription factor activity

2009

Heat shock protein 27 (HSP27) accumulates in stressed cells and helps them to survive adverse conditions. We have already shown that HSP27 has a function in the ubiquitination process that is modulated by its oligomerization/phosphorylation status. Here, we show that HSP27 is also involved in protein sumoylation, a ubiquitination-related process. HSP27 increases the number of cell proteins modified by small ubiquitin-like modifier (SUMO)-2/3 but this effect shows some selectivity as it neither affects all proteins nor concerns SUMO-1. Moreover, no such alteration in SUMO-2/3 conjugation is achievable by another HSP, such as HSP70. Heat shock factor 1 (HSF1), a transcription factor responsib…

Protein sumoylationTranscriptional ActivationCancer Researchendocrine systemanimal structuresSUMO proteinHSP27 Heat-Shock ProteinsBiologyurologic and male genital diseasesenvironment and public healthSubstrate Specificity03 medical and health sciencesTransactivation0302 clinical medicineHeat Shock Transcription FactorsHeat shock proteinGeneticsAnimalsHumansAnimals Cell Nucleus/metabolism DNA-Binding Proteins/*metabolism HSP27 Heat-Shock Proteins/chemistry/*metabolism Hela Cells Humans Protein Multimerization Protein Structure[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyHSF1Protein Structure QuaternaryMolecular BiologyTranscription factorUbiquitinsHeat-Shock Proteins030304 developmental biologyCell Nucleus0303 health sciencesMolecular biologyHsp70Cell biologyHeat shock factorDNA-Binding ProteinsProtein TransportQuaternary Protein Transport Small Ubiquitin-Related Modifier Proteins/*metabolism Substrate Specificity Transcription Factors/*metabolism Transcriptional Activation Ubiquitins/*metabolism030220 oncology & carcinogenesisembryonic structuresSmall Ubiquitin-Related Modifier ProteinsProtein MultimerizationHeLa CellsMolecular ChaperonesTranscription Factors
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DETECTION OF PLIO-QUATERNARY FAULTS IN MADONIE MOUNTAINS (SICILY) BY USING QUANTITATIVE GEOMORPHIC AND STRUCTURAL GEOLOGY ANALYSES

2011

The Northern Madonie Mountains (Northern-Central Sicily), sector of the Sicilian Maghrebian chain, consist of a tectonic thrust system developed through two subsequent main contractional events: 1) a shallow-seated compressional event developed during the Middle-Upper Miocene; 2) a deep-seated transpressional event occuring since the Late Miocene. Lower Pliocene (Trubi) to Quaternary clastic deposits unconformably lie on the tectonic units and are partially involved by deformation. In the selected area, syntectonic sedimentary basins characters are able to define the timing of deformation only until the Lower Pliocene; to resolve this gap of information application of quantitative geomorphi…

QUATERNARY TECTONICSSettore GEO/03 - Geologia StrutturaleSettore GEO/04 - Geografia Fisica E GeomorfologiaSTRUCTURAL ANALYSESQUANTITATIVE GEOMORPHIC ANALYSES NORTHERN-CENTRAL SICILY
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Incoherent elastic and quasi-elastic neutron scattering investigation of hemoglobin dynamics.

2005

In this work we investigate the dynamic properties of hemoglobin in glycerolD(8)/D(2)O solution using incoherent elastic (ENS) and quasi-elastic (QENS) neutron scattering. Taking advantage of complementary energy resolutions of backscattering spectrometers at ILL (Grenoble), we explore motions in a large space-time window, up to 1 ns and 14 A; moreover, in order to cover the harmonic and anharmonic protein dynamics regimes, the elastic experiments have been performed over the wide temperature interval of 20-300 K. To study the dependence of the measured dynamics upon the protein quaternary structure, both deoxyhemoglobin (in T quaternary conformation) and carbonmonoxyhemoglobin (in R quater…

Quantitative Biology::BiomoleculesChemistryProtein dynamicsOrganic ChemistryNeutron diffractionMomentum transferAnharmonicityBiophysicsTemperatureProtein dynamicsHemoglobin quaternary structureMean square displacementDynamical transitionNeutron scatteringBiochemistryElasticityMean squared displacementOxygenHemoglobinsNeutron DiffractionHumansDiffusion (business)Atomic physicsStructure factorHydrogenBiophysical chemistry
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Quaternary relaxations in sol-gel encapsulated hemoglobin studied via NIR and UV spectroscopy.

2007

In this work, we study the kinetics of the R --T transition in hemoglobin using a combination of near-infrared and near-ultraviolet spectroscopy. We use a sol-gel encapsulation protocol to decelerate the conformational transitions and to avoid spectral perturbations arising from ligand migration and recombination. We monitor two spectroscopic markers: band III in the near-IR, which is a fine probe of the heme pocket conformation, and the tryptophan band in the near-UV, which probes the formation of the Trpbeta37-Aspalpha94 hydrogen bond, characteristic of the T structure, at the critical alpha1beta2 subunit interface. The time evolution of these two bands is monitored after deoxygenation of…

Quantitative Biology::BiomoleculesSpectrophotometry InfraredHydrogen bondReducing agentKineticsAnalytical chemistryhemoglobinLigandsBiochemistrychemistry.chemical_compoundHemoglobinsKineticsUltraviolet visible spectroscopyMyoglobinchemistryPhysical chemistryHumansProtein quaternary structureSpectrophotometry UltravioletSpectroscopyProtein Structure QuaternaryDeoxygenationGelsProtein BindingBiochemistry
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Pylogenetic history and biogeographic aspects of fossil and extant Terricola (Mammalia, Rodentia) of Southern Italy: a case study

2009

Quaternary Terricola Endemic BiogeographySettore GEO/01 - Paleontologia E Paleoecologia
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Vertebrate biological events and Pleistocene biogeographic history of Sicily

2009

Quaternary Vertebrates Bioevents SicilySettore GEO/01 - Paleontologia E Paleoecologia
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Quaternary tectonics from landscape evolution in southern Italy: new clues from a multidisciplinary morphometric approach

2022

QuaternaryActive TectonicsSettore GEO/02 - Geologia Stratigrafica E SedimentologicaSettore GEO/03 - Geologia StrutturaleSeismotectonicsTectonic Geomorphology
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